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Volumn 48, Issue 1, 2015, Pages 35-116

Visualizing transient dark states by NMR spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

MAGNETISM; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROCEDURES; TIME;

EID: 84924003209     PISSN: 00335835     EISSN: 14698994     Source Type: Journal    
DOI: 10.1017/S0033583514000122     Document Type: Article
Times cited : (181)

References (370)
  • 2
    • 0035951101 scopus 로고    scopus 로고
    • Estimation of inter-residue distances in spin labeled proteins at physiological temperatures: Experimental strategies and practical limitations
    • ALTENBACH, C., OH, K. J., TRABANINO, R. J., HIDEG, K. & HUBBELL, W. L. (2001). Estimation of inter-residue distances in spin labeled proteins at physiological temperatures: experimental strategies and practical limitations. Biochemistry 40, 15471-15482.
    • (2001) Biochemistry , vol.40 , pp. 15471-15482
    • Altenbach, C.1    Oh, K.J.2    Trabanino, R.J.3    Hideg, K.4    Hubbell, W.L.5
  • 3
    • 84879775056 scopus 로고    scopus 로고
    • The length of the calmodulin linker determines the extent of transient interdomain association and target affinity
    • ANTHIS, N. J. & CLORE, G.M. (2013). The length of the calmodulin linker determines the extent of transient interdomain association and target affinity. Journal of American Chemical Society 135, 9648-9651.
    • (2013) Journal of American Chemical Society , vol.135 , pp. 9648-9651
    • Anthis, N.J.1    Clore, G.M.2
  • 4
    • 83055186781 scopus 로고    scopus 로고
    • Transient, sparsely populated compact states of apo and calcium-loaded calmodulin probed by paramagnetic relaxation enhancement: Interplay of conformational selection and induced fit
    • ANTHIS, N. J., DOUCLEFF, M. & CLORE, G.M. (2011). Transient, sparsely populated compact states of apo and calcium-loaded calmodulin probed by paramagnetic relaxation enhancement: interplay of conformational selection and induced fit. Journal of American Chemical Society 133, 18966-18974.
    • (2011) Journal of American Chemical Society , vol.133 , pp. 18966-18974
    • Anthis, N.J.1    Doucleff, M.2    Clore, G.M.3
  • 6
    • 0029865938 scopus 로고    scopus 로고
    • Future directions in folding: The multi-state nature of protein structure
    • BAI, Y. & ENGLANDER, S.W. (1996). Future directions in folding: the multi-state nature of protein structure. Proteins 24, 145-151.
    • (1996) Proteins , vol.24 , pp. 145-151
    • Bai, Y.1    Englander, S.W.2
  • 7
    • 33646925084 scopus 로고    scopus 로고
    • Protein folding pathways studied by pulsed-and native-state hydrogen exchange
    • BAI, Y.W. (2006). Protein folding pathways studied by pulsed-and native-state hydrogen exchange. Chemical Reviews 106, 1757-1768.
    • (2006) Chemical Reviews , vol.106 , pp. 1757-1768
    • Bai, Y.W.1
  • 8
    • 0029643523 scopus 로고
    • Protein-folding intermediates - native-state hydrogen-exchange
    • BAI, Y.W., SOSNICK, T. R., MAYNE, L. & ENGLANDER, S.W. (1995). Protein-folding intermediates - native-state hydrogen-exchange. Science 269, 192-197.
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.W.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 10
    • 84878107864 scopus 로고    scopus 로고
    • Hydrogen-exchange mass spectrometry for the study of intrinsic disorder in proteins
    • BALASUBRAMANIAM, D. & KOMIVES, E. A. (2013). Hydrogen-exchange mass spectrometry for the study of intrinsic disorder in proteins. Biochimica et Biophysica Acta 1834, 1202-1209.
    • (2013) Biochimica et Biophysica Acta , vol.1834 , pp. 1202-1209
    • Balasubramaniam, D.1    Komives, E.A.2
  • 11
    • 70350348011 scopus 로고    scopus 로고
    • NMR spectroscopy brings invisible protein states into focus
    • BALDWIN, A. J. & KAY, L. E. (2009). NMR spectroscopy brings invisible protein states into focus. Nature Chemical Biology 5, 808-814.
    • (2009) Nature Chemical Biology , vol.5 , pp. 808-814
    • Baldwin, A.J.1    Kay, L.E.2
  • 12
    • 84879552012 scopus 로고    scopus 로고
    • An R(1rho) expression for a spin in chemical exchange between two sites with unequal transverse relaxation rates
    • BALDWIN, A. J. & KAY, L. E. (2013). An R(1rho) expression for a spin in chemical exchange between two sites with unequal transverse relaxation rates. Journal of Biomolecular NMR 55, 211-218.
    • (2013) Journal of Biomolecular NMR , vol.55 , pp. 211-218
    • Baldwin, A.J.1    Kay, L.E.2
  • 13
    • 84864210811 scopus 로고    scopus 로고
    • Exceeding the limit of dynamics studies on biomolecules using high spinlock field strengths with a cryogenically cooled probehead
    • BAN, D., GOSSERT, A. D., GILLER, K., BECKER, S., GRIESINGER, C. & LEE, D. (2012). Exceeding the limit of dynamics studies on biomolecules using high spinlock field strengths with a cryogenically cooled probehead. Journal of Magnetic Resonance 221, 1-4.
    • (2012) Journal of Magnetic Resonance , vol.221 , pp. 1-4
    • Ban, D.1    Gossert, A.D.2    Giller, K.3    Becker, S.4    Griesinger, C.5    Lee, D.6
  • 15
    • 0026748968 scopus 로고
    • Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected twodimensional NMR spectroscopy: The central helix is flexible
    • BARBATO, G., IKURA, M., KAY, L. E., PASTOR, R.W. & BAX, A. (1992). Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected twodimensional NMR spectroscopy: the central helix is flexible. Biochemistry 31, 5269-5278.
    • (1992) Biochemistry , vol.31 , pp. 5269-5278
    • Barbato, G.1    Ikura, M.2    Kay, L.E.3    Pastor, R.W.4    Bax, A.5
  • 17
    • 74849106907 scopus 로고    scopus 로고
    • Visualization of the encounter ensemble of the transient electron transfer complex of cytochrome c and cytochrome c peroxidase
    • BASHIR, Q., VOLKOV, A. N., ULLMANN, G.M. & UBBINK, M. (2009). Visualization of the encounter ensemble of the transient electron transfer complex of cytochrome c and cytochrome c peroxidase. Journal of American Chemical Society 132, 241-247.
    • (2009) Journal of American Chemical Society , vol.132 , pp. 241-247
    • Bashir, Q.1    Volkov, A.N.2    Ullmann, G.M.3    Ubbink, M.4
  • 18
    • 0034625121 scopus 로고    scopus 로고
    • Utilization of sitedirected spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data
    • BATTISTE, J.L. & WAGNER, G. (2000). Utilization of sitedirected spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data. Biochemistry 39, 5355-5365.
    • (2000) Biochemistry , vol.39 , pp. 5355-5365
    • Battiste, J.L.1    Wagner, G.2
  • 19
    • 0024533979 scopus 로고
    • Characterization of a partly folded protein by NMR methods: Studies on the molten globule state of guinea pig alpha-lactalbumin
    • BAUM, J., DOBSON, C. M., EVANS, P.A. & HANLEY, C. (1989). Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig alpha-lactalbumin. Biochemistry 28, 7-13.
    • (1989) Biochemistry , vol.28 , pp. 7-13
    • Baum, J.1    Dobson, C.M.2    Evans, P.A.3    Hanley, C.4
  • 20
    • 0002240405 scopus 로고
    • Nuclear-spin relaxation in paramagnetic systems (S = 1) in the slowmotion regime for the electron-spin.4. Motional anisotropy andnNoncoinciding dipole-dipole and zerofield Splitting tensors
    • BENETIS, N. & KOWALEWSKI, J. (1985). Nuclear-spin relaxation in paramagnetic systems (S = 1) in the slowmotion regime for the electron-spin .4. Motional anisotropy andnNoncoinciding dipole-dipole and zerofield Splitting tensors. Journal of Magnetic Resonance 65, 13-33.
    • (1985) Journal of Magnetic Resonance , vol.65 , pp. 13-33
    • Benetis, N.1    Kowalewski, J.2
  • 22
    • 67650469932 scopus 로고    scopus 로고
    • Determination of the solution-bound conformation of an amino acid binding protein by NMR paramagnetic relaxation enhancement: Use of a single flexible paramagnetic probe with improved estimation of its sampling space
    • BERMEJO, G. A., STRUB, M.-P., H O, C. & TJANDRA, N. (2009). Determination of the solution-bound conformation of an amino acid binding protein by NMR paramagnetic relaxation enhancement: use of a single flexible paramagnetic probe with improved estimation of its sampling space. Journal of American Chemical Society 131, 9532-9537.
    • (2009) Journal of American Chemical Society , vol.131 , pp. 9532-9537
    • Bermejo, G.A.1    Strub, M.-P.2    Ho, C.3    Tjandra, N.4
  • 27
    • 35548988910 scopus 로고    scopus 로고
    • Paramagnetism-based NMR restraints provide maximum allowed probabilities for the different conformations of partially independent protein domains
    • BERTINI, I., GUPTA, Y. K., LUCHINAT, C., PARIGI, G., PEANA, M., SGHERI, L. & YUAN, J. (2007). Paramagnetism-based NMR restraints provide maximum allowed probabilities for the different conformations of partially independent protein domains. Journal of the American Chemical Society 129, 12786-12794.
    • (2007) Journal of the American Chemical Society , vol.129 , pp. 12786-12794
    • Bertini, I.1    Gupta, Y.K.2    Luchinat, C.3    Parigi, G.4    Peana, M.5    Sgheri, L.6    Yuan, J.7
  • 28
    • 84862303541 scopus 로고    scopus 로고
    • Paramagnetic relaxation enhancement for the characterization of the conformational heterogeneity in two-domain proteins
    • BERTINI, I., LUCHINAT, C., NAGULAPALLI, M., PARIGI, G. & RAVERA, E. (2012b). Paramagnetic relaxation enhancement for the characterization of the conformational heterogeneity in two-domain proteins. Physical Chemistry and Chemical Physics 14, 9149-9156.
    • (2012) Physical Chemistry and Chemical Physics , vol.14 , pp. 9149-9156
    • Bertini, I.1    Luchinat, C.2    Nagulapalli, M.3    Parigi, G.4    Ravera, E.5
  • 31
  • 34
    • 0011327448 scopus 로고
    • Nuclear induction
    • BLOCH, F. (1946). Nuclear induction. Physics Reviews 70, 460-474.
    • (1946) Physics Reviews , vol.70 , pp. 460-474
    • Bloch, F.1
  • 35
    • 36849117843 scopus 로고
    • Proton relaxation times in paramagnetic solutions
    • BLOEMBERGEN, N. (1957). Proton relaxation times in paramagnetic solutions. Journal of Chemical Physics 27, 572-573.
    • (1957) Journal of Chemical Physics , vol.27 , pp. 572-573
    • Bloembergen, N.1
  • 36
    • 0042033050 scopus 로고
    • Proton relaxation times in paramagnetic solutions effects of electron spin relaxation
    • BLOEMBERGEN, N. & MORGAN, L. O. (1961). Proton relaxation times in paramagnetic solutions effects of electron spin relaxation. Journal of Chemical Physics 34, 842-850.
    • (1961) Journal of Chemical Physics , vol.34 , pp. 842-850
    • Bloembergen, N.1    Morgan, L.O.2
  • 37
    • 67649380327 scopus 로고    scopus 로고
    • Multiple tight phospholipid-binding modes of alpha-synuclein revealed by solution NMR spectroscopy
    • BODNER, C. R., DOBSON, C.M. & BAX, A. (2009). Multiple tight phospholipid-binding modes of alpha-synuclein revealed by solution NMR spectroscopy. Journal of Molecular Biology 390, 775-790.
    • (2009) Journal of Molecular Biology , vol.390 , pp. 775-790
    • Bodner, C.R.1    Dobson, C.M.2    Bax, A.3
  • 38
    • 75749093356 scopus 로고    scopus 로고
    • Differential phospholipid binding of alphasynuclein variants implicated in Parkinson's disease revealed by solution NMR spectroscopy
    • BODNER, C. R., MALTSEV, A. S., DOBSON, C.M. & BAX, A. (2010). Differential phospholipid binding of alphasynuclein variants implicated in Parkinson's disease revealed by solution NMR spectroscopy. Biochemistry 49, 862-871.
    • (2010) Biochemistry , vol.49 , pp. 862-871
    • Bodner, C.R.1    Maltsev, A.S.2    Dobson, C.M.3    Bax, A.4
  • 39
    • 50849111095 scopus 로고    scopus 로고
    • Conformational relaxation following hydride transfer plays a limiting role in dihydrofolate reductase catalysis
    • BOEHR, D. D., DYSON, H.J. & WRIGHT, P. E. (2008). Conformational relaxation following hydride transfer plays a limiting role in dihydrofolate reductase catalysis. Biochemistry 47, 9227-9233.
    • (2008) Biochemistry , vol.47 , pp. 9227-9233
    • Boehr, D.D.1    Dyson, H.J.2    Wright, P.E.3
  • 40
    • 33748781457 scopus 로고    scopus 로고
    • The dynamic energy landscape of dihydrofolate reductase catalysis
    • BOEHR, D. D., MCELHENY, D., DYSON, H.J. & WRIGHT, P. E. (2006). The dynamic energy landscape of dihydrofolate reductase catalysis. Science 313, 1638-1642.
    • (2006) Science , vol.313 , pp. 1638-1642
    • Boehr, D.D.1    Mcelheny, D.2    Dyson, H.J.3    Wright, P.E.4
  • 42
    • 84865118861 scopus 로고    scopus 로고
    • A 2D 13C-CEST experiment for studying slowly exchanging protein systems using methyl probes: An application to protein folding
    • BOUVIGNIES, G. & KAY, L. E. (2012a). A 2D 13C-CEST experiment for studying slowly exchanging protein systems using methyl probes: an application to protein folding. Journal of Biomolecular NMR 53, 303-310.
    • (2012) Journal of Biomolecular NMR , vol.53 , pp. 303-310
    • Bouvignies, G.1    Kay, L.E.2
  • 43
    • 84871000000 scopus 로고    scopus 로고
    • Measurement of proton chemical shifts in invisible states of slowly exchanging protein systems by chemical exchange saturation transfer
    • BOUVIGNIES, G. & KAY, L. E. (2012b). Measurement of proton chemical shifts in invisible states of slowly exchanging protein systems by chemical exchange saturation transfer. Journal of Physical Chemistry B 116, 14311-14317.
    • (2012) Journal of Physical Chemistry B , vol.116 , pp. 14311-14317
    • Bouvignies, G.1    Kay, L.E.2
  • 44
    • 77954689925 scopus 로고    scopus 로고
    • A simple method for measuring signs of (1)H (N) chemical shift differences between ground and excited protein states
    • BOUVIGNIES, G., KORZHNEV, D. M., NEUDECKER, P., HANSEN, D. F., CORDES, M.H. & KAY, L. E. (2010). A simple method for measuring signs of (1)H (N) chemical shift differences between ground and excited protein states. Journal of Biomolecular NMR 47, 135-141.
    • (2010) Journal of Biomolecular NMR , vol.47 , pp. 135-141
    • Bouvignies, G.1    Korzhnev, D.M.2    Neudecker, P.3    Hansen, D.F.4    Cordes, M.H.5    Kay, L.E.6
  • 46
    • 84892540887 scopus 로고    scopus 로고
    • Visualizing side chains of invisible protein conformers by solution NMR
    • BOUVIGNIES, G., VALLURUPALLI, P. & KAY, L. E. (2014). Visualizing side chains of invisible protein conformers by solution NMR. Journal of Molecular Biology 426, 763-774.
    • (2014) Journal of Molecular Biology , vol.426 , pp. 763-774
    • Bouvignies, G.1    Vallurupalli, P.2    Kay, L.E.3
  • 47
    • 71149088976 scopus 로고    scopus 로고
    • Resolving conformational and rotameric exchange in spin-labeled proteins using saturation recovery EPR
    • BRIDGES, M. D., HIDEG, K. & HUBBELL, W. L. (2010). Resolving conformational and rotameric exchange in spin-labeled proteins using saturation recovery EPR. Applied Magnetic Resonance 37, 363-390.
    • (2010) Applied Magnetic Resonance , vol.37 , pp. 363-390
    • Bridges, M.D.1    Hideg, K.2    Hubbell, W.L.3
  • 48
    • 0001767250 scopus 로고
    • Influence of rapid intramolecular motion on NMR cross-relaxation rates - A molecular-dynamics study of antamanide in solution
    • BRUSCHWEILER, R., ROUX, B., BLACKLEDGE, M., GRIESINGER, C., KARPLUS, M. & ERNST, R. R. (1992). Influence of rapid intramolecular motion on NMR cross-relaxation rates - a molecular-dynamics study of antamanide in solution. Journal of American Chemical Society 114, 2289-2302.
    • (1992) Journal of American Chemical Society , vol.114 , pp. 2289-2302
    • Bruschweiler, R.1    Roux, B.2    Blackledge, M.3    Griesinger, C.4    Karplus, M.5    Ernst, R.R.6
  • 49
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein-folding - A synthesis
    • BRYNGELSON, J. D., ONUCHIC, J. N., SOCCI, N.D. & WOLYNES, P. G. (1995). Funnels, pathways, and the energy landscape of protein-folding - a synthesis. Proteins 21, 167-195.
    • (1995) Proteins , vol.21 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4
  • 51
    • 84908221627 scopus 로고    scopus 로고
    • Modelling dynamics in protein crystal structures by ensemble refinement
    • BURNLEY, B. T., AFONINE, P. V., ADAMS, P.D. & GROS, P. (2012). Modelling dynamics in protein crystal structures by ensemble refinement. eLife 1, e00311.
    • (2012) eLife , vol.1
    • Burnley, B.T.1    Afonine, P.V.2    Adams, P.D.3    Gros, P.4
  • 52
    • 0033363494 scopus 로고    scopus 로고
    • Gadolinium(III) chelates as MRI contrast agents: Structure, dynamics, and applications
    • CARAVAN, P., ELLISON, J. J., MCMURRY, T.J. & LAUFFER, R. B. (1999). Gadolinium(III) chelates as MRI contrast agents: structure, dynamics, and applications. Chemical Reviews 99, 2293-2352.
    • (1999) Chemical Reviews , vol.99 , pp. 2293-2352
    • Caravan, P.1    Ellison, J.J.2    Mcmurry, T.J.3    Lauffer, R.B.4
  • 53
    • 26244466162 scopus 로고    scopus 로고
    • Structural basis of ARNT PAS-B dimerization: Use of a common beta-sheet interface for hetero- and homodimerization
    • CARD, P. B., ERBEL, P.J.A. & GARDNER, K. H. (2005). Structural basis of ARNT PAS-B dimerization: use of a common beta-sheet interface for hetero- and homodimerization. Journal of Molecular Biology 353, 664-677.
    • (2005) Journal of Molecular Biology , vol.353 , pp. 664-677
    • Card, P.B.1    Erbel, P.J.A.2    Gardner, K.H.3
  • 54
    • 33847534249 scopus 로고
    • Effects of diffusion on free precession in nuclear magnetic resonance experiments
    • CARR, H.Y. & PURCELL, E.M. (1954). Effects of diffusion on free precession in nuclear magnetic resonance experiments. Physics Reviews 94, 630-638.
    • (1954) Physics Reviews , vol.94 , pp. 630-638
    • Carr, H.Y.1    Purcell, E.M.2
  • 55
    • 0002889918 scopus 로고
    • General 2-site solution for chemical exchange produced dependence of T2 upon Carr-Purcell pulse separation
    • CARVER, J.P. & RICHARDS, R. E. (1972). General 2-site solution for chemical exchange produced dependence of T2 upon Carr-Purcell pulse separation. Journal of Magnetic Resonance 6, 89-105.
    • (1972) Journal of Magnetic Resonance , vol.6 , pp. 89-105
    • Carver, J.P.1    Richards, R.E.2
  • 58
    • 0018736213 scopus 로고
    • Nuclear magnetic resonance studies of the binding of trimethoprim to dihydrofolate reductase
    • CAYLEY, P. J., ALBRAND, J. P., FEENEY, J., ROBERTS, G. C., PIPER, E.A. & BURGEN, A. S. (1979). Nuclear magnetic resonance studies of the binding of trimethoprim to dihydrofolate reductase. Biochemistry 18, 3886-3895.
    • (1979) Biochemistry , vol.18 , pp. 3886-3895
    • Cayley, P.J.1    Albrand, J.P.2    Feeney, J.3    Roberts, G.C.4    Piper, E.A.5    Burgen, A.S.6
  • 60
    • 0029746061 scopus 로고    scopus 로고
    • Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH
    • CHAMBERLAIN, A. K., HANDEL, T.M. & MARQUSEE, S. (1996). Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH. Nature Structural Biology 3, 782-787.
    • (1996) Nature Structural Biology , vol.3 , pp. 782-787
    • Chamberlain, A.K.1    Handel, T.M.2    Marqusee, S.3
  • 61
    • 0034581325 scopus 로고    scopus 로고
    • Comparison of equilibrium and kinetic approaches for determining protein folding mechanisms
    • CHAMBERLAIN, A.K. & MARQUSEE, S. (2000). Comparison of equilibrium and kinetic approaches for determining protein folding mechanisms. Advances in Protein Chemistry 53, 283-328.
    • (2000) Advances in Protein Chemistry , vol.53 , pp. 283-328
    • Chamberlain, A.K.1    Marqusee, S.2
  • 63
    • 77951667170 scopus 로고    scopus 로고
    • 15N H/D-SOLEXSY experiment for accurate measurement of amide solvent exchange rates: Application to denatured drkN SH3
    • CHEVELKOV, V., XUE, Y., RAO, D. K., FORMAN-KAY, J.D. & SKRYNNIKOV, N. R. (2010). 15N H/D-SOLEXSY experiment for accurate measurement of amide solvent exchange rates: application to denatured drkN SH3. Journal of Biomolecular NMR 46, 227-244.
    • (2010) Journal of Biomolecular NMR , vol.46 , pp. 227-244
    • Chevelkov, V.1    Xue, Y.2    Rao, D.K.3    Forman-Kay, J.D.4    Skrynnikov, N.R.5
  • 64
    • 0037622537 scopus 로고    scopus 로고
    • Insights into the mobility of methyl-bearing side chains in proteins from (3)J(CC) and (3)J(CN) couplings
    • CHOU, J. J., CASE, D.A. & BAX, A. (2003). Insights into the mobility of methyl-bearing side chains in proteins from (3)J(CC) and (3)J(CN) couplings. Journal of American Chemical Society 125, 8959-8966.
    • (2003) Journal of American Chemical Society , vol.125 , pp. 8959-8966
    • Chou, J.J.1    Case, D.A.2    Bax, A.3
  • 65
    • 0035906650 scopus 로고    scopus 로고
    • Calculation of ensembles of structures representing the unfolded state of an SH3 domain
    • CHOY, W.Y. & FORMAN-KAY, J. D. (2001). Calculation of ensembles of structures representing the unfolded state of an SH3 domain. Journal of Molecular Biology 308, 1011-1032.
    • (2001) Journal of Molecular Biology , vol.308 , pp. 1011-1032
    • Choy, W.Y.1    Forman-Kay, J.D.2
  • 66
    • 0037172787 scopus 로고    scopus 로고
    • Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein
    • CHU, R., PEI, W., TAKEI, J. & BAI, Y. (2002). Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry 41, 7998-8003.
    • (2002) Biochemistry , vol.41 , pp. 7998-8003
    • Chu, R.1    Pei, W.2    Takei, J.3    Bai, Y.4
  • 68
    • 0034254909 scopus 로고    scopus 로고
    • Accurate and rapid docking of protein-protein complexes on the basis of intermolecular nuclear Overhauser enhancement data and dipolar couplings by rigid body minimization
    • CLORE, G.M. (2000). Accurate and rapid docking of protein-protein complexes on the basis of intermolecular nuclear Overhauser enhancement data and dipolar couplings by rigid body minimization. Proceedings of the National Academy of Sciences of the United States of America 97, 9021-9025.
    • (2000) Proceedings of the National Academy of Sciences of the United States of America , vol.97 , pp. 9021-9025
    • Clore, G.M.1
  • 69
    • 58149354711 scopus 로고    scopus 로고
    • Visualizing lowly-populated regions of the free energy landscape of macromolecular complexes by paramagnetic relaxation enhancement
    • CLORE, G.M. (2008). Visualizing lowly-populated regions of the free energy landscape of macromolecular complexes by paramagnetic relaxation enhancement. Molecular Biosystems 4, 1058-1069.
    • (2008) Molecular Biosystems , vol.4 , pp. 1058-1069
    • Clore, G.M.1
  • 70
    • 79251586250 scopus 로고    scopus 로고
    • Exploring sparsely populated states of macromolecules by diamagnetic and paramagnetic NMR relaxation
    • CLORE, G.M. (2011). Exploring sparsely populated states of macromolecules by diamagnetic and paramagnetic NMR relaxation. Protein Science 20, 229-246.
    • (2011) Protein Science , vol.20 , pp. 229-246
    • Clore, G.M.1
  • 71
    • 84894280807 scopus 로고    scopus 로고
    • Interplay between conformational selection and induced fit in multidomain protein-ligand binding probed by paramagnetic relaxation enhancement
    • CLORE, G.M. (2013). Interplay between conformational selection and induced fit in multidomain protein-ligand binding probed by paramagnetic relaxation enhancement. Biophysical Chemistry 186, 3-12.
    • (2013) Biophysical Chemistry , vol.186 , pp. 3-12
    • Clore, G.M.1
  • 72
    • 0036018868 scopus 로고    scopus 로고
    • Using conjoined rigid body/torsion angle simulated annealing to determine the relative orientation of covalently linked protein domains from dipolar couplings
    • CLORE, G.M. & BEWLEY, C. A. (2002). Using conjoined rigid body/torsion angle simulated annealing to determine the relative orientation of covalently linked protein domains from dipolar couplings. Journal of Magnetic Resonance 154, 329-335.
    • (2002) Journal of Magnetic Resonance , vol.154 , pp. 329-335
    • Clore, G.M.1    Bewley, C.A.2
  • 73
    • 0025063347 scopus 로고
    • Analysis of the backbone dynamics of interleukin-1 beta using two-dimensional inverse detected heteronuclear 15N-1H NMR spectroscopy
    • CLORE, G. M., DRISCOLL, P. C., WINGFIELD, P.T. & GRONENBORN, A.M. (1990a). Analysis of the backbone dynamics of interleukin-1 beta using two-dimensional inverse detected heteronuclear 15N-1H NMR spectroscopy. Biochemistry 29, 7387-7401.
    • (1990) Biochemistry , vol.29 , pp. 7387-7401
    • Clore, G.M.1    Driscoll, P.C.2    Wingfield, P.T.3    Gronenborn, A.M.4
  • 74
    • 0000393431 scopus 로고
    • Theory and applications of the transferred nuclear overhauser effect to the study of the conformations of small ligands bound to proteins
    • CLORE, G.M. & GRONENBORN, A.M. (1982). Theory and applications of the transferred nuclear overhauser effect to the study of the conformations of small ligands bound to proteins. Journal of Magnetic Resonance 48, 402-417.
    • (1982) Journal of Magnetic Resonance , vol.48 , pp. 402-417
    • Clore, G.M.1    Gronenborn, A.M.2
  • 75
    • 0001342923 scopus 로고
    • Theory of the time-dependent transferred nuclear overhauser effect - applications to structural-analysis of ligand protein complexes in solution
    • CLORE, G.M. & GRONENBORN, A.M. (1983). Theory of the time-dependent transferred nuclear overhauser effect - applications to structural-analysis of ligand protein complexes in solution. Journal of Magnetic Resonance 53, 423-442.
    • (1983) Journal of Magnetic Resonance , vol.53 , pp. 423-442
    • Clore, G.M.1    Gronenborn, A.M.2
  • 76
    • 0025871254 scopus 로고
    • Structures of larger proteins in solution - 3-dimensional and 4-dimensional heteronuclear nmr-spectroscopy
    • CLORE, G.M. & GRONENBORN, A.M. (1991). Structures of larger proteins in solution - 3-dimensional and 4-dimensional heteronuclear nmr-spectroscopy. Science 252, 1390-1399.
    • (1991) Science , vol.252 , pp. 1390-1399
    • Clore, G.M.1    Gronenborn, A.M.2
  • 78
    • 70349093561 scopus 로고    scopus 로고
    • Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes
    • CLORE, G.M. & IWAHARA, J. (2009). Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes. Chemical Reviews 109, 4108-4139.
    • (2009) Chemical Reviews , vol.109 , pp. 4108-4139
    • Clore, G.M.1    Iwahara, J.2
  • 79
    • 4143079167 scopus 로고    scopus 로고
    • Amplitudes of protein backbone dynamics and correlated motions in a small alpha/beta protein: Correspondence of dipolar coupling and heteronuclear relaxation measurements
    • CLORE, G.M. & SCHWIETERS, C.D. (2004a). Amplitudes of protein backbone dynamics and correlated motions in a small alpha/beta protein: correspondence of dipolar coupling and heteronuclear relaxation measurements. Biochemistry 43, 10678-10691.
    • (2004) Biochemistry , vol.43 , pp. 10678-10691
    • Clore, G.M.1    Schwieters, C.D.2
  • 80
    • 1542317796 scopus 로고    scopus 로고
    • How much backbone motion in ubiquitin is required to account for dipolar coupling data measured in multiple alignment media as assessed by independent crossvalidation?
    • CLORE, G.M. & SCHWIETERS, C.D. (2004b). How much backbone motion in ubiquitin is required to account for dipolar coupling data measured in multiple alignment media as assessed by independent crossvalidation? Journal of American Chemical Society 126, 2923-2938.
    • (2004) Journal of American Chemical Society , vol.126 , pp. 2923-2938
    • Clore, G.M.1    Schwieters, C.D.2
  • 81
    • 29444446536 scopus 로고    scopus 로고
    • Concordance of residual dipolar couplings, backbone order parameters and crystallographic B-factors for a small alpha/beta protein: A unified picture of high probability, fast atomic motions in proteins
    • CLORE, G.M. & SCHWIETERS, C.D. (2006). Concordance of residual dipolar couplings, backbone order parameters and crystallographic B-factors for a small alpha/beta protein: a unified picture of high probability, fast atomic motions in proteins. Journal of Molecular Biology 355, 879-886.
    • (2006) Journal of Molecular Biology , vol.355 , pp. 879-886
    • Clore, G.M.1    Schwieters, C.D.2
  • 82
    • 0025046144 scopus 로고
    • Deviations from the simple two-parameter model-free approach to the interpretation of N-15 nuclear magnetic-relaxation of proteins
    • CLORE, G. M., SZABO, A., BAX, A., KAY, L. E., DRISCOLL, P.C. & GRONENBORN, A.M. (1990b). Deviations from the simple two-parameter model-free approach to the interpretation of N-15 nuclear magnetic-relaxation of proteins. Journal of American Chemical Society 112, 4989-4991.
    • (1990) Journal of American Chemical Society , vol.112 , pp. 4989-4991
    • Clore, G.M.1    Szabo, A.2    Bax, A.3    Kay, L.E.4    Driscoll, P.C.5    Gronenborn, A.M.6
  • 83
    • 35548943472 scopus 로고    scopus 로고
    • Elucidating transient macromolecular interactions using paramagnetic relaxation enhancement
    • CLORE, G. M., TANG, C. & IWAHARA, J. (2007). Elucidating transient macromolecular interactions using paramagnetic relaxation enhancement. Current Opinion in Structural Biology 17, 603-616.
    • (2007) Current Opinion in Structural Biology , vol.17 , pp. 603-616
    • Clore, G.M.1    Tang, C.2    Iwahara, J.3
  • 84
    • 0037076522 scopus 로고    scopus 로고
    • Evidence for flexibility in the function of ribonuclease A
    • COLE, R. & LORIA, J. P. (2002). Evidence for flexibility in the function of ribonuclease A. Biochemistry 41, 6072-6081.
    • (2002) Biochemistry , vol.41 , pp. 6072-6081
    • Cole, R.1    Loria, J.P.2
  • 85
    • 0035799354 scopus 로고    scopus 로고
    • Molecular motion of spin labeled side chains in alpha-helices: Analysis by variation of side chain structure
    • COLUMBUS, L., KALAI, T., JEKO, J., HIDEG, K. & HUBBELL, W. L. (2001). Molecular motion of spin labeled side chains in alpha-helices: analysis by variation of side chain structure. Biochemistry 40, 3828-3846.
    • (2001) Biochemistry , vol.40 , pp. 3828-3846
    • Columbus, L.1    Kalai, T.2    Jeko, J.3    Hideg, K.4    Hubbell, W.L.5
  • 86
    • 84901008835 scopus 로고    scopus 로고
    • The C-terminal threonine of Abeta43 nucleates toxic aggregation via structural and dynamical changes in monomers and protofibrils
    • CONICELLA, A.E. & FAWZI, N. L. (2014). The C-terminal threonine of Abeta43 nucleates toxic aggregation via structural and dynamical changes in monomers and protofibrils. Biochemistry 20, 3095-3105.
    • (2014) Biochemistry , vol.20 , pp. 3095-3105
    • Conicella, A.E.1    Fawzi, N.L.2
  • 89
    • 0028472289 scopus 로고
    • Direct measurements of the dissociation-rate constant for inhibitor-enzyme complexes via the T1 rho and T2 (CPMG) methods
    • DAVIS, D. G., PERLMAN, M.E. & LONDON, R. E. (1994). Direct measurements of the dissociation-rate constant for inhibitor-enzyme complexes via the T1 rho and T2 (CPMG) methods. Journal of Magnetic Resonance B 104, 266-275.
    • (1994) Journal of Magnetic Resonance B , vol.104 , pp. 266-275
    • Davis, D.G.1    Perlman, M.E.2    London, R.E.3
  • 93
    • 0001248067 scopus 로고
    • Studies of chemical exchange by nuclear magnetic relaxation in rotating frame
    • DEVERELL, C., MORGAN, R.E. & STRANGE, J. H. (1970). Studies of chemical exchange by nuclear magnetic relaxation in rotating frame. Molecular Physics 18, 553-559.
    • (1970) Molecular Physics , vol.18 , pp. 553-559
    • Deverell, C.1    Morgan, R.E.2    Strange, J.H.3
  • 94
    • 0030199899 scopus 로고    scopus 로고
    • Mass spectrometric determination of isotopic exchange rates of amide hydrogens located on the surfaces of proteins
    • DHARMASIRI, K. & SMITH, D. L. (1996). Mass spectrometric determination of isotopic exchange rates of amide hydrogens located on the surfaces of proteins. Analytical Chemistry 68, 2340-2344.
    • (1996) Analytical Chemistry , vol.68 , pp. 2340-2344
    • Dharmasiri, K.1    Smith, D.L.2
  • 96
    • 0037174538 scopus 로고    scopus 로고
    • Derivation of structural restraints using a thiol-reactive chelator
    • DVORETSKY, A., GAPONENKO, V. & ROSEVEAR, P. R. (2002). Derivation of structural restraints using a thiol-reactive chelator. FEBS Letters 528, 189-192.
    • (2002) FEBS Letters , vol.528 , pp. 189-192
    • Dvoretsky, A.1    Gaponenko, V.2    Rosevear, P.R.3
  • 97
    • 0026489715 scopus 로고
    • Incorporation of an EDTA-metal complex at a rationally selected site within a protein - application to EDTA-iron DNA affinity cleaving with catabolite gene activator protein (CAP) and Cro
    • EBRIGHT, Y.W., CHEN, Y., PENDERGRAST, P.S. & EBRIGHT, R. H. (1992). Incorporation of an EDTA-metal complex at a rationally selected site within a protein - application to EDTA-iron DNA affinity cleaving with catabolite gene activator protein (CAP) and Cro. Biochemistry 31, 10664-10670.
    • (1992) Biochemistry , vol.31 , pp. 10664-10670
    • Ebright, Y.W.1    Chen, Y.2    Pendergrast, P.S.3    Ebright, R.H.4
  • 98
    • 0028956081 scopus 로고
    • The energetics and dynamics of molecular recognition by calmodulin
    • EHRHARDT, M. R., URBAUER, J.L. & WAND, A. J. (1995). The energetics and dynamics of molecular recognition by calmodulin. Biochemistry 34, 2731-2738.
    • (1995) Biochemistry , vol.34 , pp. 2731-2738
    • Ehrhardt, M.R.1    Urbauer, J.L.2    Wand, A.J.3
  • 99
    • 33846505918 scopus 로고    scopus 로고
    • Observation of microsecond time-scale protein dynamics in the presence of Ln3+ ions: Application to the N-terminal domain of cardiac troponin C
    • EICHMULLER, C. & SKRYNNIKOV, N. R. (2007). Observation of microsecond time-scale protein dynamics in the presence of Ln3+ ions: application to the N-terminal domain of cardiac troponin C. Journal of Biomolecular NMR 37, 79-95.
    • (2007) Journal of Biomolecular NMR , vol.37 , pp. 79-95
    • Eichmuller, C.1    Skrynnikov, N.R.2
  • 102
    • 33750320427 scopus 로고    scopus 로고
    • Hydrogen exchange and mass spectrometry: A historical perspective
    • ENGLANDER, S.W. (2006). Hydrogen exchange and mass spectrometry: a historical perspective. Journal of American Society for Mass Spectrometry 17, 1481-1489.
    • (2006) Journal of American Society for Mass Spectrometry , vol.17 , pp. 1481-1489
    • Englander, S.W.1
  • 103
    • 0020855355 scopus 로고
    • Hydrogen exchange and structural dynamics of proteins and nucleic acids
    • ENGLANDER, S.W.&KALLENBACH, N. R. (1983). Hydrogen exchange and structural dynamics of proteins and nucleic acids. Quarterly Reviews of Biophysics 16, 521-655.
    • (1983) Quarterly Reviews of Biophysics , vol.16 , pp. 521-655
    • Englander, S.W.1    Kallenbach, N.R.2
  • 104
    • 0030612609 scopus 로고    scopus 로고
    • Hydrogen exchange: The modern legacy of Linderstrom-Lang
    • ENGLANDER, S.W., MAYNE, L., BAI, Y. & SOSNICK, T.R. (1997). Hydrogen exchange: the modern legacy of Linderstrom-Lang. Protein Science 6, 1101-1109.
    • (1997) Protein Science , vol.6 , pp. 1101-1109
    • Englander, S.W.1    Mayne, L.2    Bai, Y.3    Sosnick, T.R.4
  • 107
    • 3342925849 scopus 로고    scopus 로고
    • Methods to study protein dynamics and folding by mass spectrometry
    • EYLES, S. J. & KALTASHOV, I. A. (2004). Methods to study protein dynamics and folding by mass spectrometry. Methods 34, 88-99.
    • (2004) Methods , vol.34 , pp. 88-99
    • Eyles, S.J.1    Kaltashov, I.A.2
  • 108
    • 0028503463 scopus 로고
    • A heteronuclear correlation experiment for simultaneous determination of 15N longitudinal decay and chemical exchange rates of systems in slow equilibrium
    • FARROW, N. A., ZHANG, O., FORMAN-KAY, J.D. & KAY, L. E. (1994). A heteronuclear correlation experiment for simultaneous determination of 15N longitudinal decay and chemical exchange rates of systems in slow equilibrium. Journal of Biomolecular NMR 4, 727-734.
    • (1994) Journal of Biomolecular NMR , vol.4 , pp. 727-734
    • Farrow, N.A.1    Zhang, O.2    Forman-Kay, J.D.3    Kay, L.E.4
  • 111
    • 84908480411 scopus 로고    scopus 로고
    • Characterizing methyl-bearing sidechain contacts and dynamics mediating amyloid β protofibril interactions using 13Cmethyl-DEST and lifetime line broadening
    • FAWZI, N. L., LIBICH, D. S., YING, J., TUGARINOV, V. & CLORE, G.M. (2014). Characterizing methyl-bearing sidechain contacts and dynamics mediating amyloid β protofibril interactions using 13Cmethyl-DEST and lifetime line broadening. Angewandte Chimie International Edition 53, 10345-10349.
    • (2014) Angewandte Chimie International Edition , vol.53 , pp. 10345-10349
    • Fawzi, N.L.1    Libich, D.S.2    Ying, J.3    Tugarinov, V.4    Clore, G.M.5
  • 112
    • 83055176454 scopus 로고    scopus 로고
    • Atomic-resolution dynamics on the surface of amyloid β protofibrils probed by solution NMR
    • FAWZI, N. L., YING, J., GHIRLANDO, R., TORCHIA, D.A. & CLORE, G.M. (2011b). Atomic-resolution dynamics on the surface of amyloid β protofibrils probed by solution NMR. Nature 480, 268-272.
    • (2011) Nature , vol.480 , pp. 268-272
    • Fawzi, N.L.1    Ying, J.2    Ghirlando, R.3    Torchia, D.A.4    Clore, G.M.5
  • 114
    • 84864482745 scopus 로고    scopus 로고
    • Probing exchange kinetics and atomic resolution dynamics in high-molecular-weight complexes using dark-state exchange saturation transfer NMR spectroscopy
    • FAWZI, N. L., YING, J., TORCHIA, D.A. & CLORE, G.M. (2012). Probing exchange kinetics and atomic resolution dynamics in high-molecular-weight complexes using dark-state exchange saturation transfer NMR spectroscopy. Nature Protocols 7, 1523-1533.
    • (2012) Nature Protocols , vol.7 , pp. 1523-1533
    • Fawzi, N.L.1    Ying, J.2    Torchia, D.A.3    Clore, G.M.4
  • 116
    • 27744531924 scopus 로고    scopus 로고
    • The energy landscape of modular repeat proteins: Topology determines folding mechanism in the ankyrin family
    • FERREIRO, D. U., CHO, S. S., KOMIVES, E.A. & WOLYNES, P. G. (2005). The energy landscape of modular repeat proteins: topology determines folding mechanism in the ankyrin family. Journal of Molecular Biology 354, 679-692.
    • (2005) Journal of Molecular Biology , vol.354 , pp. 679-692
    • Ferreiro, D.U.1    Cho, S.S.2    Komives, E.A.3    Wolynes, P.G.4
  • 117
    • 0000779478 scopus 로고
    • Identification of solvent-exposed regions of enzyme-bound ligands by nuclear-magnetic-resonance
    • FESIK, S.W., GEMMECKER, G., OLEJNICZAK, E.T. & PETROS, A.M. (1991). Identification of solvent-exposed regions of enzyme-bound ligands by nuclear-magnetic-resonance. Journal of American Chemical Society 113, 7080-7081.
    • (1991) Journal of American Chemical Society , vol.113 , pp. 7080-7081
    • Fesik, S.W.1    Gemmecker, G.2    Olejniczak, E.T.3    Petros, A.M.4
  • 118
    • 79958037883 scopus 로고    scopus 로고
    • Constructing ensembles for intrinsically disordered proteins
    • FISHER, C.K. & STULTZ, C.M. (2011). Constructing ensembles for intrinsically disordered proteins. Current Opinion in Structural Biology 21, 426-431.
    • (2011) Current Opinion in Structural Biology , vol.21 , pp. 426-431
    • Fisher, C.K.1    Stultz, C.M.2
  • 119
    • 79952124237 scopus 로고    scopus 로고
    • Measuring rapid hydrogen exchange in the homodimeric 36 kDa HIV-1 integrase catalytic core domain
    • FITZKEE, N. C., TORCHIA, D.A. & BAX, A. (2011). Measuring rapid hydrogen exchange in the homodimeric 36 kDa HIV-1 integrase catalytic core domain. Protein Science 20, 500-512.
    • (2011) Protein Science , vol.20 , pp. 500-512
    • Fitzkee, N.C.1    Torchia, D.A.2    Bax, A.3
  • 122
    • 0029938988 scopus 로고    scopus 로고
    • Crystallographic characterization of geometry and conformation of TOAC, a nitroxide spin-labelled C-alpha, C-alpha-disubstituted glycine, in simple derivatives and model peptides
    • FLIPPEN-ANDERSON, J. L., GEORGE, C., VALLE, G., VALENTE, E., BIANCO, A., FORMAGGIO, F., CRISMA, M. & TONIOLO, C. (1996). Crystallographic characterization of geometry and conformation of TOAC, a nitroxide spin-labelled C-alpha, C-alpha-disubstituted glycine, in simple derivatives and model peptides. International Journal of Peptide and Protein Research 47, 231-238.
    • (1996) International Journal of Peptide and Protein Research , vol.47 , pp. 231-238
    • Flippen-Anderson, J.L.1    George, C.2    Valle, G.3    Valente, E.4    Bianco, A.5    Formaggio, F.6    Crisma, M.7    Toniolo, C.8
  • 124
    • 33846851242 scopus 로고
    • Study of moderately rapid chemical exchange reactions by means of nuclear magnetic double resonance
    • FORSÉN, S. & HOFFMAN, R. A. (1963). Study of moderately rapid chemical exchange reactions by means of nuclear magnetic double resonance. Journal of Chemical Physics 39, 2892-2901.
    • (1963) Journal of Chemical Physics , vol.39 , pp. 2892-2901
    • ForsÉn, S.1    Hoffman, R.A.2
  • 125
    • 84882890430 scopus 로고    scopus 로고
    • Conformational freedom of metalloproteins revealed by paramagnetism-assisted NMR
    • FRAGAI, M., LUCHINAT, C., PARIGI, G. & RAVERA, E. (2013). Conformational freedom of metalloproteins revealed by paramagnetism-assisted NMR. Coordination Chemistry Reviews 257, 2652-2667.
    • (2013) Coordination Chemistry Reviews , vol.257 , pp. 2652-2667
    • Fragai, M.1    Luchinat, C.2    Parigi, G.3    Ravera, E.4
  • 126
    • 71449103005 scopus 로고    scopus 로고
    • Hidden alternative structures of proline isomerase essential for catalysis
    • FRASER, J. S., CLARKSON, M.W., DEGNAN, S. C., ERION, R., KERN, D. & ALBER, T. (2009). Hidden alternative structures of proline isomerase essential for catalysis. Nature 462, 669-673.
    • (2009) Nature , vol.462 , pp. 669-673
    • Fraser, J.S.1    Clarkson, M.W.2    Degnan, S.C.3    Erion, R.4    Kern, D.5    Alber, T.6
  • 127
    • 36749113906 scopus 로고
    • Dynamic effects of pair correlationfunctions on spin relaxation by translational diffusion in liquids.2. Finite jumps and independent T1 processes
    • FREED, J. H. (1978). Dynamic effects of pair correlationfunctions on spin relaxation by translational diffusion in liquids .2. Finite jumps and independent T1 processes. Journal of Chemical Physics 68, 4034-4037.
    • (1978) Journal of Chemical Physics , vol.68 , pp. 4034-4037
    • Freed, J.H.1
  • 128
    • 77249173821 scopus 로고    scopus 로고
    • Indirect detection of labile solute proton spectra via the water signal using frequency-labeled exchange (FLEX) transfer
    • FRIEDMAN, J. I., MCMAHON, M. T., STIVERS, J.T. & VAN ZIJL, P. C. (2010). Indirect detection of labile solute proton spectra via the water signal using frequency-labeled exchange (FLEX) transfer. Journal of American Chemical Society 132, 1813-1815.
    • (2010) Journal of American Chemical Society , vol.132 , pp. 1813-1815
    • Friedman, J.I.1    Mcmahon, M.T.2    Stivers, J.T.3    Van Zijl, P.C.4
  • 129
    • 0032539953 scopus 로고    scopus 로고
    • Local dynamics and stability of apocytochrome b562 examined by hydrogen exchange
    • FUENTES, E. J. & WAND, A. J. (1998a). Local dynamics and stability of apocytochrome b562 examined by hydrogen exchange. Biochemistry 37, 3687-3698.
    • (1998) Biochemistry , vol.37 , pp. 3687-3698
    • Fuentes, E.J.1    Wand, A.J.2
  • 130
    • 0032516448 scopus 로고    scopus 로고
    • Local stability and dynamics of apocytochrome b562 examined by the dependence of hydrogen exchange on hydrostatic pressure
    • FUENTES, E. J. & WAND, A. J. (1998b). Local stability and dynamics of apocytochrome b562 examined by the dependence of hydrogen exchange on hydrostatic pressure. Biochemistry 37, 9877-9883.
    • (1998) Biochemistry , vol.37 , pp. 9877-9883
    • Fuentes, E.J.1    Wand, A.J.2
  • 132
    • 18744361937 scopus 로고    scopus 로고
    • Reconstruction of orientations of a moving protein domain from paramagnetic data
    • GARDNER, R. J., LONGINETTI, M. & SGHERI, L. (2005). Reconstruction of orientations of a moving protein domain from paramagnetic data. Inverse Problems 21, 879.
    • (2005) Inverse Problems , vol.21 , pp. 879
    • Gardner, R.J.1    Longinetti, M.2    Sgheri, L.3
  • 133
    • 0031585990 scopus 로고    scopus 로고
    • Characterization of long-range structure in the denatured state of staphylococcal nuclease. I. Paramagnetic relaxation enhancement by nitroxide spin labels
    • GILLESPIE, J.R. & SHORTLE, D. (1997a). Characterization of long-range structure in the denatured state of staphylococcal nuclease. I. Paramagnetic relaxation enhancement by nitroxide spin labels. Journal of Molecular Biology 268, 158-169.
    • (1997) Journal of Molecular Biology , vol.268 , pp. 158-169
    • Gillespie, J.R.1    Shortle, D.2
  • 134
    • 0031585992 scopus 로고    scopus 로고
    • Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures
    • GILLESPIE, J.R. & SHORTLE, D. (1997b). Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures. Journal of Molecular Biology 268, 170-184.
    • (1997) Journal of Molecular Biology , vol.268 , pp. 170-184
    • Gillespie, J.R.1    Shortle, D.2
  • 135
    • 33750705653 scopus 로고    scopus 로고
    • A century of Alzheimer's disease
    • GOEDERT, M. & SPILLANTINI, M. G. (2006). A century of Alzheimer's disease. Science 314, 777-781.
    • (2006) Science , vol.314 , pp. 777-781
    • Goedert, M.1    Spillantini, M.G.2
  • 136
    • 84861980106 scopus 로고    scopus 로고
    • Requirements on paramagnetic relaxation enhancement data for membrane protein structure determination by NMR
    • GOTTSTEIN, D., RECKEL, S., DOTSCH, V. & GUNTERT, P. (2012). Requirements on paramagnetic relaxation enhancement data for membrane protein structure determination by NMR. Structure 20, 1019-1027.
    • (2012) Structure , vol.20 , pp. 1019-1027
    • Gottstein, D.1    Reckel, S.2    Dotsch, V.3    Guntert, P.4
  • 138
    • 84866414232 scopus 로고    scopus 로고
    • Contrast-matched small-angle X-ray scattering from a heavy-atom labeled protein in structure determination: Application to a lead-substituted calmodulin-peptide complex
    • GRISHAEV, A., ANTHIS, N.J. & CLORE, G.M. (2012). Contrast-matched small-angle X-ray scattering from a heavy-atom labeled protein in structure determination: application to a lead-substituted calmodulin-peptide complex. Journal of American Chemical Society 134, 14686-14689.
    • (2012) Journal of American Chemical Society , vol.134 , pp. 14686-14689
    • Grishaev, A.1    Anthis, N.J.2    Clore, G.M.3
  • 139
    • 0347281686 scopus 로고    scopus 로고
    • Ribosome loading onto the mRNA cap is driven by conformational coupling between eIF4 G and eIF4E
    • GROSS, J. D., MOERKE, N. J., VON DER HAAR, T., LUGOVSKOY, A. A., SACHS, A. B., MCCARTHY, J.E.G. & WAGNER, G. (2003). Ribosome loading onto the mRNA cap is driven by conformational coupling between eIF4 G and eIF4E. Cell 115, 739-750.
    • (2003) Cell , vol.115 , pp. 739-750
    • Gross, J.D.1    Moerke, N.J.2    Von Der Haar, T.3    Lugovskoy, A.A.4    Sachs, A.B.5    Mccarthy, J.E.G.6    Wagner, G.7
  • 140
    • 0002711832 scopus 로고
    • Nuclear-relaxation in macromolecules by paramagnetic-ions - novel mechanism
    • GUERON, M. (1975). Nuclear-relaxation in macromolecules by paramagnetic-ions - novel mechanism. Journal of Magnetic Resonance 19, 58-66.
    • (1975) Journal of Magnetic Resonance , vol.19 , pp. 58-66
    • Gueron, M.1
  • 141
    • 0014954355 scopus 로고
    • Double nuclear magnetic resonance observation of electron exchange between ferri- and ferrocytochrome c
    • GUPTA, R.K. & REDFIELD, A. G. (1970). Double nuclear magnetic resonance observation of electron exchange between ferri- and ferrocytochrome c. Science 169, 1204-1206.
    • (1970) Science , vol.169 , pp. 1204-1206
    • Gupta, R.K.1    Redfield, A.G.2
  • 143
    • 84856912378 scopus 로고    scopus 로고
    • Quantifying millisecond exchange dynamics in proteins by CPMG relaxation dispersion NMR using side-chain 1H probes
    • HANSEN, A. L., LUNDSTROM, P., VELYVIS, A. & KAY, L.E. (2012). Quantifying millisecond exchange dynamics in proteins by CPMG relaxation dispersion NMR using side-chain 1H probes. Journal of American Chemical Society 134, 3178-3189.
    • (2012) Journal of American Chemical Society , vol.134 , pp. 3178-3189
    • Hansen, A.L.1    Lundstrom, P.2    Velyvis, A.3    Kay, L.E.4
  • 144
    • 67849097846 scopus 로고    scopus 로고
    • Extending the range of microsecond-to-millisecond chemical exchange detected in labeled and unlabeled nucleic acids by selective carbon R1(rho) NMR spectroscopy
    • HANSEN, A. L., NIKOLOVA, E. N., CASIANO-NEGRONI, A. & AL-HASHIMI, H.M. (2009). Extending the range of microsecond-to-millisecond chemical exchange detected in labeled and unlabeled nucleic acids by selective carbon R1(rho) NMR spectroscopy. Journal of American Chemical Society 131, 3818-3819.
    • (2009) Journal of American Chemical Society , vol.131 , pp. 3818-3819
    • Hansen, A.L.1    Nikolova, E.N.2    Casiano-Negroni, A.3    Al-Hashimi, H.M.4
  • 145
    • 46949093335 scopus 로고    scopus 로고
    • Using relaxation dispersion NMR spectroscopy to determine structures of excited, invisible protein states
    • HANSEN, D. F., VALLURUPALLI, P. & KAY, L. E. (2008a). Using relaxation dispersion NMR spectroscopy to determine structures of excited, invisible protein states. Journal of Biomolecular NMR 41, 113-120.
    • (2008) Journal of Biomolecular NMR , vol.41 , pp. 113-120
    • Hansen, D.F.1    Vallurupalli, P.2    Kay, L.E.3
  • 146
    • 39749156063 scopus 로고    scopus 로고
    • Probing chemical shifts of invisible states of proteins with relaxation dispersion NMR spectroscopy: How well can we do?
    • HANSEN, D. F., VALLURUPALLI, P., LUNDSTROM, P., NEUDECKER, P. & KAY, L. E. (2008b). Probing chemical shifts of invisible states of proteins with relaxation dispersion NMR spectroscopy: how well can we do? Journal of American Chemical Society 130, 2667-2675.
    • (2008) Journal of American Chemical Society , vol.130 , pp. 2667-2675
    • Hansen, D.F.1    Vallurupalli, P.2    Lundstrom, P.3    Neudecker, P.4    Kay, L.E.5
  • 148
    • 77955809772 scopus 로고    scopus 로고
    • Validation of a lanthanide tag for the analysis of protein dynamics by paramagnetic NMR spectroscopy
    • HASS, M. A., KEIZERS, P. H., BLOK, A., HIRUMA, Y. & UBBINK, M. (2010). Validation of a lanthanide tag for the analysis of protein dynamics by paramagnetic NMR spectroscopy. Journal of American Chemical Society 132, 9952-9953.
    • (2010) Journal of American Chemical Society , vol.132 , pp. 9952-9953
    • Hass, M.A.1    Keizers, P.H.2    Blok, A.3    Hiruma, Y.4    Ubbink, M.5
  • 149
    • 70350066141 scopus 로고    scopus 로고
    • DOTA-M8: An extremely rigid, high-affinity lanthanide chelating tag for PCS NMR spectroscopy
    • HAUSSINGER, D., HUANG, J.R. & GRZESIEK, S. (2009). DOTA-M8: an extremely rigid, high-affinity lanthanide chelating tag for PCS NMR spectroscopy. Journal of American Chemical Society 131, 14761-14767.
    • (2009) Journal of American Chemical Society , vol.131 , pp. 14761-14767
    • Haussinger, D.1    Huang, J.R.2    Grzesiek, S.3
  • 150
    • 0033792053 scopus 로고    scopus 로고
    • Simulations of NMR pulse sequences during equilibrium and non-equilibrium chemical exchange
    • HELGSTRAND, M., HARD, T. & ALLARD, P. (2000). Simulations of NMR pulse sequences during equilibrium and non-equilibrium chemical exchange. Journal of Biomolecular NMR 18, 49-63.
    • (2000) Journal of Biomolecular NMR , vol.18 , pp. 49-63
    • Helgstrand, M.1    Hard, T.2    Allard, P.3
  • 151
    • 0037165571 scopus 로고    scopus 로고
    • O2 penetration and proton burial depth in proteins: Applicability to fold family recognition
    • HERNANDEZ, G., TENG, C. L., BRYANT, R.G. & LEMASTER, D.M. (2002). O2 penetration and proton burial depth in proteins: applicability to fold family recognition. Journal of American Chemical Society 124, 4463-4472.
    • (2002) Journal of American Chemical Society , vol.124 , pp. 4463-4472
    • Hernandez, G.1    Teng, C.L.2    Bryant, R.G.3    Lemaster, D.M.4
  • 152
    • 0035312659 scopus 로고    scopus 로고
    • Recent advances in FRET: Distance determination in protein-DNA complexes
    • HILLISCH, A., LORENZ, M. & DIEKMANN, S. (2001). Recent advances in FRET: distance determination in protein-DNA complexes. Current Opinion in Structural Biology 11, 201-207.
    • (2001) Current Opinion in Structural Biology , vol.11 , pp. 201-207
    • Hillisch, A.1    Lorenz, M.2    Diekmann, S.3
  • 153
    • 0032574796 scopus 로고    scopus 로고
    • Pressure dependence of amide hydrogen-deuterium exchange rates for individual sites in T4 lysozyme
    • HITCHENS, T.K. & BRYANT, R. G. (1998). Pressure dependence of amide hydrogen-deuterium exchange rates for individual sites in T4 lysozyme. Biochemistry 37, 5878-5887.
    • (1998) Biochemistry , vol.37 , pp. 5878-5887
    • Hitchens, T.K.1    Bryant, R.G.2
  • 154
    • 70350020881 scopus 로고    scopus 로고
    • Chaperonin-mediated protein folding: Using a central cavity to kinetically assist polypeptide chain folding
    • HORWICH, A.L. & FENTON, W. A. (2009). Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding. Quarterly Reviews of Biophysics 42, 83-116.
    • (2009) Quarterly Reviews of Biophysics , vol.42 , pp. 83-116
    • Horwich, A.L.1    Fenton, W.A.2
  • 155
    • 34247860719 scopus 로고    scopus 로고
    • Spin-state selective carbon-detected HNCO with TROSY optimization in all dimensions and double echo-antiecho sensitivity enhancement in both indirect dimensions
    • HU, K., VOGELI, B. & CLORE, G.M. (2007). Spin-state selective carbon-detected HNCO with TROSY optimization in all dimensions and double echo-antiecho sensitivity enhancement in both indirect dimensions. Journal of American Chemical Society 129, 5484-5491.
    • (2007) Journal of American Chemical Society , vol.129 , pp. 5484-5491
    • Hu, K.1    Vogeli, B.2    Clore, G.M.3
  • 156
    • 84889573110 scopus 로고    scopus 로고
    • Bioconjugation of proteins with a paramagnetic NMR and fluorescent tag
    • HUANG, F., PEI, Y. Y., ZUO, H. H., CHEN, J. L., YANG, Y. & SU, X. C. (2013). Bioconjugation of proteins with a paramagnetic NMR and fluorescent tag. Chemistry 19, 17141-17149.
    • (2013) Chemistry , vol.19 , pp. 17141-17149
    • Huang, F.1    Pei, Y.Y.2    Zuo, H.H.3    Chen, J.L.4    Yang, Y.5    Su, X.C.6
  • 157
    • 0033812585 scopus 로고    scopus 로고
    • Identifying conformational changes with site-directed spin labeling
    • HUBBELL, W. L., CAFISO, D.S. & ALTENBACH, C. (2000). Identifying conformational changes with site-directed spin labeling. Nature Structural Biology 7, 735-739.
    • (2000) Nature Structural Biology , vol.7 , pp. 735-739
    • Hubbell, W.L.1    Cafiso, D.S.2    Altenbach, C.3
  • 159
    • 0025186451 scopus 로고
    • Structural characterization of a partly folded apomyoglobin intermediate
    • HUGHSON, F. M., WRIGHT, P.E. & BALDWIN, R. L. (1990). Structural characterization of a partly folded apomyoglobin intermediate. Science 249, 1544-1548.
    • (1990) Science , vol.249 , pp. 1544-1548
    • Hughson, F.M.1    Wright, P.E.2    Baldwin, R.L.3
  • 160
    • 0000807746 scopus 로고
    • Dynamic effects of pair correlation-functions on spin relaxation by translational diffusion in liquids
    • HWANG, L.P. & FREED, J. H. (1975). Dynamic effects of pair correlation-functions on spin relaxation by translational diffusion in liquids. Journal of Chemical Physics 63, 4017-4025.
    • (1975) Journal of Chemical Physics , vol.63 , pp. 4017-4025
    • Hwang, L.P.1    Freed, J.H.2
  • 161
    • 33646945580 scopus 로고    scopus 로고
    • Characterization of the fast dynamics of protein amino acid side chains using NMR relaxation in solution
    • IGUMENOVA, T. I., FREDERICK, K.K. & WAND, A. J. (2006). Characterization of the fast dynamics of protein amino acid side chains using NMR relaxation in solution. Chemical Reviews 106, 1672-1699.
    • (2006) Chemical Reviews , vol.106 , pp. 1672-1699
    • Igumenova, T.I.1    Frederick, K.K.2    Wand, A.J.3
  • 163
    • 0026536335 scopus 로고
    • Solution structure of a calmodulin-target peptide complex by multidimensional NMR
    • IKURA, M., CLORE, G. M., GRONENBORN, A. M., ZHU, G., KLEE, C.B. & BAX, A. (1992). Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science 256, 632-638.
    • (1992) Science , vol.256 , pp. 632-638
    • Ikura, M.1    Clore, G.M.2    Gronenborn, A.M.3    Zhu, G.4    Klee, C.B.5    Bax, A.6
  • 165
    • 0033200247 scopus 로고    scopus 로고
    • Flap opening and dimerinterface flexibility in the free and inhibitor-bound HIV protease, and their implications for function
    • ISHIMA, R., FREEDBERG, D. I., WANG, Y. X., LOUIS, J.M. & TORCHIA, D. A. (1999). Flap opening and dimerinterface flexibility in the free and inhibitor-bound HIV protease, and their implications for function. Structure 7, 1047-1055.
    • (1999) Structure , vol.7 , pp. 1047-1055
    • Ishima, R.1    Freedberg, D.I.2    Wang, Y.X.3    Louis, J.M.4    Torchia, D.A.5
  • 166
    • 0032871220 scopus 로고    scopus 로고
    • Estimating the time scale of chemical exchange of proteins from measurements of transverse relaxation rates in solution
    • ISHIMA, R. & TORCHIA, D. A. (1999). Estimating the time scale of chemical exchange of proteins from measurements of transverse relaxation rates in solution. Journal of Biomolecular NMR 14, 369-372.
    • (1999) Journal of Biomolecular NMR , vol.14 , pp. 369-372
    • Ishima, R.1    Torchia, D.A.2
  • 168
    • 0037355721 scopus 로고    scopus 로고
    • Extending the range of amide proton relaxation dispersion experiments in proteins using a constant-time relaxation-compensated CPMG approach
    • ISHIMA, R. & TORCHIA, D. A. (2003). Extending the range of amide proton relaxation dispersion experiments in proteins using a constant-time relaxation-compensated CPMG approach. Journal of BiomolecularNMR 25, 243-248.
    • (2003) Journal of BiomolecularNMR , vol.25 , pp. 243-248
    • Ishima, R.1    Torchia, D.A.2
  • 169
    • 0037533875 scopus 로고    scopus 로고
    • EDTA-derivatized deoxythymidine as a tool for rapid determination of protein binding polarity to DNA by intermolecular paramagnetic relaxation enhancement
    • IWAHARA, J., ANDERSON, D. E., MURPHY, E.C. & CLORE, G.M. (2003). EDTA-derivatized deoxythymidine as a tool for rapid determination of protein binding polarity to DNA by intermolecular paramagnetic relaxation enhancement. Journal of American Chemical Society 125, 6634-6635.
    • (2003) Journal of American Chemical Society , vol.125 , pp. 6634-6635
    • Iwahara, J.1    Anderson, D.E.2    Murphy, E.C.3    Clore, G.M.4
  • 170
    • 33646356250 scopus 로고    scopus 로고
    • Detecting transient intermediates in macromolecular binding by paramagnetic NMR
    • IWAHARA, J. & CLORE, G.M. (2006a). Detecting transient intermediates in macromolecular binding by paramagnetic NMR. Nature 440, 1227-1230.
    • (2006) Nature , vol.440 , pp. 1227-1230
    • Iwahara, J.1    Clore, G.M.2
  • 171
    • 31544448614 scopus 로고    scopus 로고
    • Direct observation of enhanced translocation of a homeodomain between DNA cognate sites by NMR exchange spectroscopy
    • IWAHARA, J. & CLORE, G.M. (2006b). Direct observation of enhanced translocation of a homeodomain between DNA cognate sites by NMR exchange spectroscopy. Journal of American Chemical Society 128, 404-405.
    • (2006) Journal of American Chemical Society , vol.128 , pp. 404-405
    • Iwahara, J.1    Clore, G.M.2
  • 172
    • 77957124004 scopus 로고    scopus 로고
    • Structure-independent analysis of the breadth of the positional distribution of disordered groups in macromolecules from order parameters for long, variable-length vectors using NMR paramagnetic relaxation enhancement
    • IWAHARA, J. & CLORE, G.M. (2010). Structure-independent analysis of the breadth of the positional distribution of disordered groups in macromolecules from order parameters for long, variable-length vectors using NMR paramagnetic relaxation enhancement. Journal of American Chemical Society 132, 13346-13356.
    • (2010) Journal of American Chemical Society , vol.132 , pp. 13346-13356
    • Iwahara, J.1    Clore, G.M.2
  • 173
    • 5644226078 scopus 로고    scopus 로고
    • Characterization of nonspecific protein-DNA interactions by H-1 paramagnetic relaxation enhancement
    • IWAHARA, J., SCHWIETERS, C.D. & CLORE, G.M. (2004a). Characterization of nonspecific protein-DNA interactions by H-1 paramagnetic relaxation enhancement. Journal of American Chemical Society 126, 12800-12808.
    • (2004) Journal of American Chemical Society , vol.126 , pp. 12800-12808
    • Iwahara, J.1    Schwieters, C.D.2    Clore, G.M.3
  • 174
    • 2442433447 scopus 로고    scopus 로고
    • Ensemble approach for NMR structure refinement against (1)H paramagnetic relaxation enhancement data arising from a flexible paramagnetic group attached to a macromolecule
    • IWAHARA, J., SCHWIETERS, C.D. & CLORE, G.M. (2004b). Ensemble approach for NMR structure refinement against (1)H paramagnetic relaxation enhancement data arising from a flexible paramagnetic group attached to a macromolecule. Journal of American Chemical Society 126, 5879-5896.
    • (2004) Journal of American Chemical Society , vol.126 , pp. 5879-5896
    • Iwahara, J.1    Schwieters, C.D.2    Clore, G.M.3
  • 175
    • 33846561471 scopus 로고    scopus 로고
    • Practical aspects of (1)H transverse paramagnetic relaxation enhancement measurements on macromolecules
    • IWAHARA, J., TANG, C. & CLORE, G.M. (2007). Practical aspects of (1)H transverse paramagnetic relaxation enhancement measurements on macromolecules. Journal of Magnetic Resonance 184, 185-195.
    • (2007) Journal of Magnetic Resonance , vol.184 , pp. 185-195
    • Iwahara, J.1    Tang, C.2    Clore, G.M.3
  • 177
    • 0034775555 scopus 로고    scopus 로고
    • Distance mapping of proteinbinding sites using spin-labeled oligosaccharide ligands
    • JAIN, N. U., VENOT, A., UMEMOTO, K., LEFFLER, H. & PRESTEGARD, J. H. (2001). Distance mapping of proteinbinding sites using spin-labeled oligosaccharide ligands. Protein Science 10, 2393-2400.
    • (2001) Protein Science , vol.10 , pp. 2393-2400
    • Jain, N.U.1    Venot, A.2    Umemoto, K.3    Leffler, H.4    Prestegard, J.H.5
  • 178
    • 0001766423 scopus 로고
    • Chemical exchange and NMR T2 relaxation - Multisite case
    • JEN, J. (1978). Chemical exchange and NMR T2 relaxation - multisite case. Journal of Magnetic Resonance 30, 111-128.
    • (1978) Journal of Magnetic Resonance , vol.30 , pp. 111-128
    • Jen, J.1
  • 179
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • JENNINGS, P.A. & WRIGHT, P. E. (1993). Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science 262, 892-896.
    • (1993) Science , vol.262 , pp. 892-896
    • Jennings, P.A.1    Wright, P.E.2
  • 180
    • 1842503161 scopus 로고    scopus 로고
    • Binding ability of a HHP-tagged protein towards Ni2+ studied by paramagnetic NMR relaxation: The possibility of obtaining long-range structure information
    • JENSEN, M. R., LAURITZEN, C., DAHL, S.W., PEDERSEN, J. & LED, J. J. (2004). Binding ability of a HHP-tagged protein towards Ni2+ studied by paramagnetic NMR relaxation: the possibility of obtaining long-range structure information. Journal of Biomolecular. NMR 29, 175-185.
    • (2004) Journal of Biomolecular. NMR , vol.29 , pp. 175-185
    • Jensen, M.R.1    Lauritzen, C.2    Dahl, S.W.3    Pedersen, J.4    Led, J.J.5
  • 181
    • 84885587001 scopus 로고    scopus 로고
    • Conformational dynamics and distribution of nitroxide spin labels
    • JESCHKE, G. (2013). Conformational dynamics and distribution of nitroxide spin labels. Progress in Nuclear Magnetic Resonance Spectroscopy 72, 42-60.
    • (2013) Progress in Nuclear Magnetic Resonance Spectroscopy , vol.72 , pp. 42-60
    • Jeschke, G.1
  • 182
    • 0033515440 scopus 로고    scopus 로고
    • The cellulosebinding domains from Cellulomonas fimi beta-1,4-glucanase CenC bind nitroxide spin-labeled cellooligosaccharides in multiple orientations
    • JOHNSON, P. E., BRUN, E., MACKENZIE, L.F., WITHERS, S.G. & MCINTOSH, L. P. (1999). The cellulosebinding domains from Cellulomonas fimi beta-1,4-glucanase CenC bind nitroxide spin-labeled cellooligosaccharides in multiple orientations. Journal of Molecular Biology 287, 609-625.
    • (1999) Journal of Molecular Biology , vol.287 , pp. 609-625
    • Johnson, P.E.1    Brun, E.2    Mackenzie, L.F.3    Withers, S.G.4    Mcintosh, L.P.5
  • 186
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • KAY, L. E., KEIFER, P. & SAARINEN, T. (1992). Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. Journal of American Chemical Society 114, 10663-10665.
    • (1992) Journal of American Chemical Society , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 187
    • 0024449503 scopus 로고
    • Backbone dynamics of proteins as studied by N-15 inverse detected heteronuclear NMR-spectroscopy - application to Staphylococcal nuclease
    • KAY, L. E., TORCHIA, D.A. & BAX, A. (1989). Backbone dynamics of proteins as studied by N-15 inverse detected heteronuclear NMR-spectroscopy - application to Staphylococcal nuclease. Biochemistry 28, 8972-8979.
    • (1989) Biochemistry , vol.28 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 190
    • 55549133637 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of a lanthanide chelating protein probe: CLaNP-5 yields predictable paramagnetic effects independent of environment
    • KEIZERS, P. H. J., SARAGLIADIS, A., HIRUMA, Y., OVERHAND, M. & UBBINK, M. (2008). Design, synthesis, and evaluation of a lanthanide chelating protein probe: CLaNP-5 yields predictable paramagnetic effects independent of environment. Journal of American Chemical Society 130, 14802-14812.
    • (2008) Journal of American Chemical Society , vol.130 , pp. 14802-14812
    • Keizers, P.H.J.1    Saragliadis, A.2    Hiruma, Y.3    Overhand, M.4    Ubbink, M.5
  • 192
    • 35448961949 scopus 로고    scopus 로고
    • Methods and applications of site-directed spin labeling EPR spectroscopy
    • KLUG, C. S. & FEIX, J. B. (2008). Methods and applications of site-directed spin labeling EPR spectroscopy. Methods in Cell Biology 84, 617-658.
    • (2008) Methods in Cell Biology , vol.84 , pp. 617-658
    • Klug, C.S.1    Feix, J.B.2
  • 193
    • 49549086897 scopus 로고    scopus 로고
    • Protein structure and dynamics studied by mass spectrometry: H/D exchange, hydroxyl radical labeling, and related approaches
    • KONERMANN, L., TONG, X. & PAN, Y. (2008). Protein structure and dynamics studied by mass spectrometry: H/D exchange, hydroxyl radical labeling, and related approaches. Journal of Mass Spectrometry 43, 1021-1036.
    • (2008) Journal of Mass Spectrometry , vol.43 , pp. 1021-1036
    • Konermann, L.1    Tong, X.2    Pan, Y.3
  • 194
    • 42449102160 scopus 로고    scopus 로고
    • Probing invisible, low-populated states of protein molecules by relaxation dispersion NMR spectroscopy: An application to protein folding
    • KORZHNEV, D.M. & KAY, L. E. (2008). Probing invisible, low-populated states of protein molecules by relaxation dispersion NMR spectroscopy: an application to protein folding. Accounts of Chemical Research 41, 442-451.
    • (2008) Accounts of Chemical Research , vol.41 , pp. 442-451
    • Korzhnev, D.M.1    Kay, L.E.2
  • 195
    • 1642416319 scopus 로고    scopus 로고
    • Probing slow dynamics in high molecular weight proteins by methyl-TROSY NMR spectroscopy: Application to a 723-residue enzyme
    • KORZHNEV, D. M., KLOIBER, K., KANELIS, V., TUGARINOV, V. & KAY, L. E. (2004a). Probing slow dynamics in high molecular weight proteins by methyl-TROSY NMR spectroscopy: application to a 723-residue enzyme. Journal of American Chemical Society 126, 3964-3973.
    • (2004) Journal of American Chemical Society , vol.126 , pp. 3964-3973
    • Korzhnev, D.M.1    Kloiber, K.2    Kanelis, V.3    Tugarinov, V.4    Kay, L.E.5
  • 196
    • 33748675500 scopus 로고    scopus 로고
    • Abp1p and fyn SH3 domains fold through similar low-populated intermediate states
    • KORZHNEV, D. M., NEUDECKER, P., ZARRINE-AFSAR, A., DAVIDSON, A.R. & KAY, L. E. (2006). Abp1p and fyn SH3 domains fold through similar low-populated intermediate states. Biochemistry 45, 10175-10183.
    • (2006) Biochemistry , vol.45 , pp. 10175-10183
    • Korzhnev, D.M.1    Neudecker, P.2    Zarrine-Afsar, A.3    Davidson, A.R.4    Kay, L.E.5
  • 197
    • 77956501272 scopus 로고    scopus 로고
    • A transient and lowpopulated protein-folding intermediate at atomic resolution
    • KORZHNEV, D. M., RELIGA, T. L., BANACHEWICZ, W., FERSHT, A.R. & KAY, L. E. (2010). A transient and lowpopulated protein-folding intermediate at atomic resolution. Science 329, 1312-1316.
    • (2010) Science , vol.329 , pp. 1312-1316
    • Korzhnev, D.M.1    Religa, T.L.2    Banachewicz, W.3    Fersht, A.R.4    Kay, L.E.5
  • 199
    • 0024853292 scopus 로고
    • Spin labeling of proteins
    • KOSEN, P. A. (1989). Spin labeling of proteins. Methods in Enzymology 177, 86-121.
    • (1989) Methods in Enzymology , vol.177 , pp. 86-121
    • Kosen, P.A.1
  • 201
    • 3342993181 scopus 로고    scopus 로고
    • Hydrogen exchange methods to study protein folding
    • KRISHNA, M. M., HOANG, L., LIN, Y. & ENGLANDER, S.W. (2004a). Hydrogen exchange methods to study protein folding. Methods 34, 51-64.
    • (2004) Methods , vol.34 , pp. 51-64
    • Krishna, M.M.1    Hoang, L.2    Lin, Y.3    Englander, S.W.4
  • 202
    • 0242578172 scopus 로고    scopus 로고
    • Intimate view of a kinetic protein folding intermediate: Residue-resolved structure, interactions, stability, folding and unfolding rates, homogeneity
    • KRISHNA, M. M., LIN, Y., MAYNE, L. & ENGLANDER, S.W. (2003). Intimate view of a kinetic protein folding intermediate: residue-resolved structure, interactions, stability, folding and unfolding rates, homogeneity. Journal of Molecular Biology 334, 501-513.
    • (2003) Journal of Molecular Biology , vol.334 , pp. 501-513
    • Krishna, M.M.1    Lin, Y.2    Mayne, L.3    Englander, S.W.4
  • 203
    • 3342993181 scopus 로고    scopus 로고
    • Hydrogen exchange methods to study protein folding
    • KRISHNA, M.M. G., HOANG, L., LIN, Y. & ENGLANDER, S.W. (2004b). Hydrogen exchange methods to study protein folding. Methods 34, 51-64.
    • (2004) Methods , vol.34 , pp. 51-64
    • Krishna, M.M.G.1    Hoang, L.2    Lin, Y.3    Englander, S.W.4
  • 204
    • 15244342213 scopus 로고    scopus 로고
    • Formation of native and non-native interactions in ensembles of denatured ACBP molecules from paramagnetic relaxation enhancement studies
    • KRISTJANSDOTTIR, S., LINDORFF-LARSEN, K., FIEBER, W., DOBSON, C. M., VENDRUSCOLO, M. & POULSEN, F.M. (2005). Formation of native and non-native interactions in ensembles of denatured ACBP molecules from paramagnetic relaxation enhancement studies. Journal of Molecular Biology 347, 1053-1062.
    • (2005) Journal of Molecular Biology , vol.347 , pp. 1053-1062
    • Kristjansdottir, S.1    Lindorff-Larsen, K.2    Fieber, W.3    Dobson, C.M.4    Vendruscolo, M.5    Poulsen, F.M.6
  • 206
    • 80755187533 scopus 로고    scopus 로고
    • The feasibility of parameterizing four-state equilibria using relaxation dispersion measurements
    • LI, P., MARTINS, I.R. & ROSEN, M. K. (2011). The feasibility of parameterizing four-state equilibria using relaxation dispersion measurements. Journal of Biomolecular NMR 51, 57-70.
    • (2011) Journal of Biomolecular NMR , vol.51 , pp. 57-70
    • Li, P.1    Martins, I.R.2    Rosen, M.K.3
  • 207
    • 33645472931 scopus 로고    scopus 로고
    • Site-directed parallel spin-labeling and paramagnetic relaxation enhancement in structure determination of membrane proteins by solution NMR spectroscopy
    • LIANG, B. Y., BUSHWELLER, J.H. & TAMM, L. K. (2006). Site-directed parallel spin-labeling and paramagnetic relaxation enhancement in structure determination of membrane proteins by solution NMR spectroscopy. Journal of American Chemical Society 128, 4389-4397.
    • (2006) Journal of American Chemical Society , vol.128 , pp. 4389-4397
    • Liang, B.Y.1    Bushweller, J.H.2    Tamm, L.K.3
  • 210
    • 46949092098 scopus 로고    scopus 로고
    • Mobility of TOAC spin-labelled peptides binding to the Src SH3 domain studied by paramagnetic NMR
    • LINDFORS, H. E., DE KONING, P. E., DRIJFHOUT, J.W., VENEZIA, B. & UBBINK, M. (2008). Mobility of TOAC spin-labelled peptides binding to the Src SH3 domain studied by paramagnetic NMR. Journal of Biomolecular NMR 41, 157-167.
    • (2008) Journal of Biomolecular NMR , vol.41 , pp. 157-167
    • Lindfors, H.E.1    De Koning, P.E.2    Drijfhout, J.W.3    Venezia, B.4    Ubbink, M.5
  • 211
    • 79951580611 scopus 로고    scopus 로고
    • Linker length dependent binding of a focal adhesion kinase derived peptide to the Src SH3-SH2 domains
    • LINDFORS, H. E., VENKATA, B. S., DRIJFHOUT, J.W. & UBBINK, M. (2011). Linker length dependent binding of a focal adhesion kinase derived peptide to the Src SH3-SH2 domains. FEBS Letters 585, 601-605.
    • (2011) FEBS Letters , vol.585 , pp. 601-605
    • Lindfors, H.E.1    Venkata, B.S.2    Drijfhout, J.W.3    Ubbink, M.4
  • 212
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules.1. Theory and range of validity
    • LIPARI, G. & SZABO, A. (1982a). Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules .1. Theory and range of validity. Journal of American Chemical Society 104, 4546-4559.
    • (1982) Journal of American Chemical Society , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 213
    • 33845553743 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules.2. Analysis of experimental results
    • LIPARI, G. & SZABO, A. (1982b). Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules .2. Analysis of experimental results. Journal of American Chemical Society 104, 4559-4570.
    • (1982) Journal of American Chemical Society , vol.104 , pp. 4559-4570
    • Lipari, G.1    Szabo, A.2
  • 215
    • 84896084604 scopus 로고    scopus 로고
    • Subtle dynamics of holo glutamine binding protein revealed with a rigid paramagnetic probe
    • LIU, Z., GONG, Z., GUO, D. C., ZHANG, W.P. & TANG, C. (2014). Subtle dynamics of holo glutamine binding protein revealed with a rigid paramagnetic probe. Biochemistry 53, 1403-1409.
    • (2014) Biochemistry , vol.53 , pp. 1403-1409
    • Liu, Z.1    Gong, Z.2    Guo, D.C.3    Zhang, W.P.4    Tang, C.5
  • 218
    • 33746283923 scopus 로고    scopus 로고
    • Efficient determination of the most favoured orientations of protein domains from paramagnetic NMR data
    • LONGINETTI, M., LUCHINAT, C., PARIGI, G. & SGHERI, L. (2006). Efficient determination of the most favoured orientations of protein domains from paramagnetic NMR data. Inverse Problems 22, 1485.
    • (2006) Inverse Problems , vol.22 , pp. 1485
    • Longinetti, M.1    Luchinat, C.2    Parigi, G.3    Sgheri, L.4
  • 219
    • 40549133186 scopus 로고    scopus 로고
    • Characterization of enzyme motions by solution NMR relaxation dispersion
    • LORIA, J. P., BERLOW, R.B. & WATT, E. D. (2008). Characterization of enzyme motions by solution NMR relaxation dispersion. Accounts of Chemical Research 41, 214-221.
    • (2008) Accounts of Chemical Research , vol.41 , pp. 214-221
    • Loria, J.P.1    Berlow, R.B.2    Watt, E.D.3
  • 220
    • 84857046973 scopus 로고    scopus 로고
    • Maximum occurrence analysis of protein conformations for different distributions of paramagnetic metal ions within flexible two-domain proteins
    • LUCHINAT, C., NAGULAPALLI, M., PARIGI, G. & SGHERI, L. (2012). Maximum occurrence analysis of protein conformations for different distributions of paramagnetic metal ions within flexible two-domain proteins. Journal of Magnetic Resonance 215, 85-93.
    • (2012) Journal of Magnetic Resonance , vol.215 , pp. 85-93
    • Luchinat, C.1    Nagulapalli, M.2    Parigi, G.3    Sgheri, L.4
  • 221
    • 24744459108 scopus 로고    scopus 로고
    • Microsecond protein dynamics measured by 13Calpha rotating-frame spin relaxation
    • LUNDSTROM, P. & AKKE, M. (2005). Microsecond protein dynamics measured by 13Calpha rotating-frame spin relaxation. Chembiochem 6, 1685-1692.
    • (2005) Chembiochem , vol.6 , pp. 1685-1692
    • Lundstrom, P.1    Akke, M.2
  • 222
    • 67749143936 scopus 로고    scopus 로고
    • Accurate measurement of alpha proton chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy
    • LUNDSTROM, P., HANSEN, D. F., VALLURUPALLI, P. & KAY, L. E. (2009a). Accurate measurement of alpha proton chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy. Journal of American Chemical Society 131, 1915-1926.
    • (2009) Journal of American Chemical Society , vol.131 , pp. 1915-1926
    • Lundstrom, P.1    Hansen, D.F.2    Vallurupalli, P.3    Kay, L.E.4
  • 223
    • 67649392285 scopus 로고    scopus 로고
    • Measuring C-13(beta) chemical shifts of invisible excited states in proteins by relaxation dispersion NMR spectroscopy
    • LUNDSTROM, P., LIN, H. & KAY, L. E. (2009b). Measuring C-13(beta) chemical shifts of invisible excited states in proteins by relaxation dispersion NMR spectroscopy. Journal of Biomolecular NMR 44, 139-155.
    • (2009) Journal of Biomolecular NMR , vol.44 , pp. 139-155
    • Lundstrom, P.1    Lin, H.2    Kay, L.E.3
  • 227
    • 0034674922 scopus 로고    scopus 로고
    • Binding orientation of proline-rich peptides in solution: Polarity of the profilin-ligand interaction
    • MAHONEY, N. M., RASTOGI, V. K., CAHILL, S. M., GIRVIN, M.E. & ALMO, S. C. (2000). Binding orientation of proline-rich peptides in solution: polarity of the profilin-ligand interaction. Journal of American Chemical Society 122, 7851-7852.
    • (2000) Journal of American Chemical Society , vol.122 , pp. 7851-7852
    • Mahoney, N.M.1    Rastogi, V.K.2    Cahill, S.M.3    Girvin, M.E.4    Almo, S.C.5
  • 229
    • 0037184479 scopus 로고    scopus 로고
    • The ATCUN domain as a probe of intermolecular interactions: Application to calmodulin-peptide complexes
    • MAL, T. K., IKURA, M. & KAY, L. E. (2002). The ATCUN domain as a probe of intermolecular interactions: application to calmodulin-peptide complexes. Journal of American Chemical Society 124, 14002-14003.
    • (2002) Journal of American Chemical Society , vol.124 , pp. 14002-14003
    • Mal, T.K.1    Ikura, M.2    Kay, L.E.3
  • 230
    • 67650684936 scopus 로고    scopus 로고
    • Structure and disorder in an unfolded state under nondenaturing conditions from ensemble models consistent with a large number of experimental restraints
    • MARSH, J.A. & FORMAN-KAY, J. D. (2009). Structure and disorder in an unfolded state under nondenaturing conditions from ensemble models consistent with a large number of experimental restraints. Journal of Molecular Biology 391, 359-374.
    • (2009) Journal of Molecular Biology , vol.391 , pp. 359-374
    • Marsh, J.A.1    Forman-Kay, J.D.2
  • 231
    • 33947133083 scopus 로고    scopus 로고
    • Improved structural characterizations of the drkN SH3 domain unfolded state suggest a compact ensemble with native-like and non-native structure
    • MARSH, J. A., NEALE, C., JACK, F. E., CHOY, W.-Y., LEE, A. Y., CROWHURST, K.A. & FORMAN-KAY, J.D. (2007). Improved structural characterizations of the drkN SH3 domain unfolded state suggest a compact ensemble with native-like and non-native structure. Journal of Molecular Biology 367, 1494-1510.
    • (2007) Journal of Molecular Biology , vol.367 , pp. 1494-1510
    • Marsh, J.A.1    Neale, C.2    Jack, F.E.3    Choy, W.-Y.4    Lee, A.Y.5    Crowhurst, K.A.6    Forman-Kay, J.D.7
  • 232
    • 0033553844 scopus 로고    scopus 로고
    • Characterization of ligand binding by saturation transfer difference NMR spectroscopy
    • MAYER, M. & MEYER, B. (1999). Characterization of ligand binding by saturation transfer difference NMR spectroscopy. Angewandte Chemie International Edition English 38, 1784-1788.
    • (1999) Angewandte Chemie International Edition English , vol.38 , pp. 1784-1788
    • Mayer, M.1    Meyer, B.2
  • 233
    • 0010957050 scopus 로고
    • Reaction rates by nuclear magnetic resonance
    • MCCONNELL, H.M. (1958). Reaction rates by nuclear magnetic resonance. Journal of Chemical Physics 28, 430-431.
    • (1958) Journal of Chemical Physics , vol.28 , pp. 430-431
    • Mcconnell, H.M.1
  • 234
    • 0026794065 scopus 로고
    • Target enzyme recognition by calmodulin: 2•4 A structure of a calmodulin-peptide complex
    • MEADOR, W. E., MEANS, A.R. & QUIOCHO, F. A. (1992). Target enzyme recognition by calmodulin: 2•4 A structure of a calmodulin-peptide complex. Science 257, 1251-1255.
    • (1992) Science , vol.257 , pp. 1251-1255
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 235
    • 36849120169 scopus 로고
    • Nuclear magnetic resonance study of proton transfer in water
    • MEIBOOM, S. (1961). Nuclear magnetic resonance study of proton transfer in water. Journal of Chemical Physics 34, 375.
    • (1961) Journal of Chemical Physics , vol.34 , pp. 375
    • Meiboom, S.1
  • 236
    • 0002899752 scopus 로고
    • Modified spin-echo method for measuring nuclear relaxation times
    • MEIBOOM, S. & GILL, D. (1958). Modified spin-echo method for measuring nuclear relaxation times. Reviews of Scientific Instruments 29, 688-691.
    • (1958) Reviews of Scientific Instruments , vol.29 , pp. 688-691
    • Meiboom, S.1    Gill, D.2
  • 237
  • 238
    • 33645834303 scopus 로고    scopus 로고
    • New tools provide new insights in NMR studies of protein dynamics
    • MITTERMAIER, A. & KAY, L. E. (2006). New tools provide new insights in NMR studies of protein dynamics. Science 312, 224-228.
    • (2006) Science , vol.312 , pp. 224-228
    • Mittermaier, A.1    Kay, L.E.2
  • 239
    • 70449769332 scopus 로고    scopus 로고
    • Observing biological dynamics at atomic resolution using NMR
    • MITTERMAIER, A.K. & KAY, L. E. (2009). Observing biological dynamics at atomic resolution using NMR. Trends in Biochemical Sciences 34, 601-611.
    • (2009) Trends in Biochemical Sciences , vol.34 , pp. 601-611
    • Mittermaier, A.K.1    Kay, L.E.2
  • 241
    • 13444305369 scopus 로고    scopus 로고
    • Simple energy landscape model for the kinetics of functional transitions in proteins
    • MIYASHITA, O., WOLYNES, P.G. & ONUCHIC, J. N. (2005). Simple energy landscape model for the kinetics of functional transitions in proteins. Journal of Physical Chemistry B 109, 1959-1969.
    • (2005) Journal of Physical Chemistry B , vol.109 , pp. 1959-1969
    • Miyashita, O.1    Wolynes, P.G.2    Onuchic, J.N.3
  • 242
    • 0032978256 scopus 로고    scopus 로고
    • Determining the occurrence of a 3(10)-helix and an alpha-helix in two different segments of a lipopeptaibol antibiotic using TOAC, a nitroxide spin-labeled C-alpha-tetrasubstituted alpha-amino acid
    • MONACO, V., FORMAGGIO, F., CRISMA, M., TONIOLO, C., HANSON, P., MILLHAUSER, G., GEORGE, C., DESCHAMPS, J.R. & FLIPPEN-ANDERSON, J. L. (1999a). Determining the occurrence of a 3(10)-helix and an alpha-helix in two different segments of a lipopeptaibol antibiotic using TOAC, a nitroxide spin-labeled C-alpha-tetrasubstituted alpha-amino acid. Bioorganic and Medicinal Chemistry 7, 119-131.
    • (1999) Bioorganic and Medicinal Chemistry , vol.7 , pp. 119-131
    • Monaco, V.1    Formaggio, F.2    Crisma, M.3    Toniolo, C.4    Hanson, P.5    Millhauser, G.6    George, C.7    Deschamps, J.R.8    Flippen-Anderson, J.L.9
  • 243
    • 0033198081 scopus 로고    scopus 로고
    • Orientation and immersion depth of a helical lipopeptaibol in membranes using TOAC as an ESR probe
    • MONACO, V., FORMAGGIO, F., CRISMA, M., TONIOLO, C., HANSON, P. & MILLHAUSER, G. L. (1999b). Orientation and immersion depth of a helical lipopeptaibol in membranes using TOAC as an ESR probe. Biopolymers 50, 239-253.
    • (1999) Biopolymers , vol.50 , pp. 239-253
    • Monaco, V.1    Formaggio, F.2    Crisma, M.3    Toniolo, C.4    Hanson, P.5    Millhauser, G.L.6
  • 245
    • 80755125957 scopus 로고    scopus 로고
    • Evaluation of the influence of intermolecular electron-nucleus couplings and intrinsic metal binding sites on the measurement of 15N longitudinal paramagnetic relaxation enhancements in proteins by solid-state NMR
    • NADAUD, P. S., SENGUPTA, I., HELMUS, J.J. & JARONIEC, C. P. (2011). Evaluation of the influence of intermolecular electron-nucleus couplings and intrinsic metal binding sites on the measurement of 15N longitudinal paramagnetic relaxation enhancements in proteins by solid-state NMR. Journal of Biomolecular NMR 51, 293-302.
    • (2011) Journal of Biomolecular NMR , vol.51 , pp. 293-302
    • Nadaud, P.S.1    Sengupta, I.2    Helmus, J.J.3    Jaroniec, C.P.4
  • 247
    • 66149129565 scopus 로고    scopus 로고
    • Relaxation dispersion NMR spectroscopy as a tool for detailed studies of protein folding
    • NEUDECKER, P., LUNDSTROM, P. & KAY, L. E. (2009). Relaxation dispersion NMR spectroscopy as a tool for detailed studies of protein folding. Biophysical Journal 96, 2045-2054.
    • (2009) Biophysical Journal , vol.96 , pp. 2045-2054
    • Neudecker, P.1    Lundstrom, P.2    Kay, L.E.3
  • 250
    • 71749087100 scopus 로고    scopus 로고
    • Quantitative description of backbone conformational sampling of unfolded proteins at amino acid resolution from NMR residual dipolar couplings
    • NODET, G., SALMON, L., OZENNE, V., MEIER, S., JENSEN, M.R. & BLACKLEDGE, M. (2009). Quantitative description of backbone conformational sampling of unfolded proteins at amino acid resolution from NMR residual dipolar couplings. Journal of American Chemical Society 131, 17908-17918.
    • (2009) Journal of American Chemical Society , vol.131 , pp. 17908-17918
    • Nodet, G.1    Salmon, L.2    Ozenne, V.3    Meier, S.4    Jensen, M.R.5    Blackledge, M.6
  • 251
    • 79951920302 scopus 로고    scopus 로고
    • A general approach for prediction of motional EPR spectra from Molecular Dynamics (MD) simulations: Application to spin labelled protein
    • OGANESYAN, V. S. (2011). A general approach for prediction of motional EPR spectra from Molecular Dynamics (MD) simulations: application to spin labelled protein. Physical Chemistry and Chemical Physics 13, 4724-4737.
    • (2011) Physical Chemistry and Chemical Physics , vol.13 , pp. 4724-4737
    • Oganesyan, V.S.1
  • 253
    • 0021114569 scopus 로고
    • 'Molten-globule state': A compact form of globular proteins with mobile sidechains
    • OHGUSHI, M. & WADA, A. (1983). 'Molten-globule state': a compact form of globular proteins with mobile sidechains. FEBS Letters 164, 21-24.
    • (1983) FEBS Letters , vol.164 , pp. 21-24
    • Ohgushi, M.1    Wada, A.2
  • 254
    • 0021754836 scopus 로고
    • Motional averaging of proton nuclear Overhauser effects in proteins - predictions from a molecular-dynamics simulation of lysozyme
    • OLEJNICZAK, E. T., DOBSON, C. M., KARPLUS, M. & LEVY, R.M. (1984). Motional averaging of proton nuclear Overhauser effects in proteins - predictions from a molecular-dynamics simulation of lysozyme. Journal of American Chemical Society 106, 1923-1930.
    • (1984) Journal of American Chemical Society , vol.106 , pp. 1923-1930
    • Olejniczak, E.T.1    Dobson, C.M.2    Karplus, M.3    Levy, R.M.4
  • 255
    • 0346421111 scopus 로고    scopus 로고
    • Magnetic resonance realization of decoherence-free quantum computation
    • OLLERENSHAW, J. E., LIDAR, D.A. & KAY, L. E. (2003). Magnetic resonance realization of decoherence-free quantum computation. Physics Reviews Letters 91, 217904.
    • (2003) Physics Reviews Letters , vol.91 , pp. 217904
    • Ollerenshaw, J.E.1    Lidar, D.A.2    Kay, L.E.3
  • 257
    • 78649509231 scopus 로고    scopus 로고
    • Probing microsecond time scale dynamics in proteins by methyl 1H-Carr-Purcell-Meiboom-Gill relaxation dispersion NMR measurements. Application to activation of the signaling protein NtrC(r)
    • OTTEN, R., VILLALI, J., KERN, D. & MULDER, F. A. (2010). Probing microsecond time scale dynamics in proteins by methyl 1H-Carr-Purcell-Meiboom-Gill relaxation dispersion NMR measurements. Application to activation of the signaling protein NtrC(r). Journal of American Chemical Society 132, 17004-17014.
    • (2010) Journal of American Chemical Society , vol.132 , pp. 17004-17014
    • Otten, R.1    Villali, J.2    Kern, D.3    Mulder, F.A.4
  • 258
    • 77952915958 scopus 로고    scopus 로고
    • Protein NMR using paramagnetic ions
    • OTTING, G. (2010). Protein NMR using paramagnetic ions. Annual Review of Biophysics 39, 387-405.
    • (2010) Annual Review of Biophysics , vol.39 , pp. 387-405
    • Otting, G.1
  • 260
    • 84896955793 scopus 로고    scopus 로고
    • Chemical exchange in biomacromolecules: Past, present, and future
    • PALMER, A. G. III (2014). Chemical exchange in biomacromolecules: past, present, and future. Journal of Magnetic Resonance 241, 3-17.
    • (2014) Journal of Magnetic Resonance , vol.241 , pp. 3-17
    • Palmer, A.G.1
  • 261
    • 16244365477 scopus 로고    scopus 로고
    • Solution NMR spin relaxation methods for characterizing chemical exchange in high-molecular-weight systems
    • PALMER, A. G. III, GREY, M.J. & WANG, C. (2005). Solution NMR spin relaxation methods for characterizing chemical exchange in high-molecular-weight systems. Methods in Enzymology 394, 430-465.
    • (2005) Methods in Enzymology , vol.394 , pp. 430-465
    • Palmer, A.G.1    Grey, M.J.2    Wang, C.3
  • 262
    • 0034919305 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules
    • PALMER, A. G. III, KROENKE, C.D. & LORIA, J. P. (2001). Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules. Methods in Enzymology 339, 204-238.
    • (2001) Methods in Enzymology , vol.339 , pp. 204-238
    • Palmer, A.G.1    Kroenke, C.D.2    Loria, J.P.3
  • 263
    • 33744908076 scopus 로고    scopus 로고
    • Characterization of the dynamics of biomacromolecules using rotatingframe spin relaxation NMR spectroscopy
    • PALMER, A. G. III & MASSI, F. (2006). Characterization of the dynamics of biomacromolecules using rotatingframe spin relaxation NMR spectroscopy. Chemical Reviews 106, 1700-1719.
    • (2006) Chemical Reviews , vol.106 , pp. 1700-1719
    • Palmer, A.G.1    Massi, F.2
  • 264
    • 67650992092 scopus 로고    scopus 로고
    • Structure and flexibility within proteins as identified through small angle X-ray scattering
    • PELIKAN, M., HURA, G.L. & HAMMEL, M. (2009). Structure and flexibility within proteins as identified through small angle X-ray scattering. General Physiology and Biophysics 28, 174-189.
    • (2009) General Physiology and Biophysics , vol.28 , pp. 174-189
    • Pelikan, M.1    Hura, G.L.2    Hammel, M.3
  • 265
    • 0028674384 scopus 로고
    • Investigation of protein motions via relaxation measurements
    • PENG, J.W. &WAGNER, G. (1994). Investigation of protein motions via relaxation measurements. Methods in Enzymology 239, 563-596.
    • (1994) Methods in Enzymology , vol.239 , pp. 563-596
    • Peng, J.W.1    Wagner, G.2
  • 266
    • 47249159078 scopus 로고    scopus 로고
    • A soluble oligomer of tau associated with fiber formation analyzed by NMR
    • PETERSON, D.W., ZHOU, H., DAHLQUIST, F.W. & LEW, J. (2008). A soluble oligomer of tau associated with fiber formation analyzed by NMR. Biochemistry 47, 7393-7404.
    • (2008) Biochemistry , vol.47 , pp. 7393-7404
    • Peterson, D.W.1    Zhou, H.2    Dahlquist, F.W.3    Lew, J.4
  • 267
    • 0025153333 scopus 로고
    • NMR identification of protein surfaces using paramagnetic probes
    • PETROS, A. M., MUELLER, L. & KOPPLE, K.D. (1990). NMR identification of protein surfaces using paramagnetic probes. Biochemistry 29, 10041-10048.
    • (1990) Biochemistry , vol.29 , pp. 10041-10048
    • Petros, A.M.1    Mueller, L.2    Kopple, K.D.3
  • 268
    • 9544231680 scopus 로고    scopus 로고
    • Modulation of the distance dependence of paramagnetic relaxation enhancements by CSA × DSA cross-correlation
    • PINTACUDA, G., KAIKKONEN, A. & OTTING, G. (2004a). Modulation of the distance dependence of paramagnetic relaxation enhancements by CSA × DSA cross-correlation. Journal of Magnetic Resonance 171, 233-243.
    • (2004) Journal of Magnetic Resonance , vol.171 , pp. 233-243
    • Pintacuda, G.1    Kaikkonen, A.2    Otting, G.3
  • 270
    • 0037160426 scopus 로고    scopus 로고
    • Identification of protein surfaces by NMR measurements with a paramagnetic Gd(III) chelate
    • PINTACUDA, G. & OTTING, G. (2002). Identification of protein surfaces by NMR measurements with a paramagnetic Gd(III) chelate. Journal of American Chemical Society 124, 372-373.
    • (2002) Journal of American Chemical Society , vol.124 , pp. 372-373
    • Pintacuda, G.1    Otting, G.2
  • 272
    • 0141987859 scopus 로고    scopus 로고
    • Exchange-transferred NOE spectroscopy and bound ligand structure determination
    • POST, C. B. (2003). Exchange-transferred NOE spectroscopy and bound ligand structure determination. Current Opinion in Structural Biology 13, 581-588.
    • (2003) Current Opinion in Structural Biology , vol.13 , pp. 581-588
    • Post, C.B.1
  • 273
    • 0032576150 scopus 로고    scopus 로고
    • A new method to detect long-range protein-RNA contacts: NMR detection of electron-proton relaxation induced by nitroxide spinlabeled RNA
    • RAMOS, A. & VARANI, G. (1998). A new method to detect long-range protein-RNA contacts: NMR detection of electron-proton relaxation induced by nitroxide spinlabeled RNA. Journal of American Chemical Society 120, 10992-10993.
    • (1998) Journal of American Chemical Society , vol.120 , pp. 10992-10993
    • Ramos, A.1    Varani, G.2
  • 274
    • 0024404656 scopus 로고
    • Nuclear magnetic resonance line-shape analysis and determination of exchange rates
    • RAO, B. D. (1989). Nuclear magnetic resonance line-shape analysis and determination of exchange rates. Methods in Enzymology 176, 279-311.
    • (1989) Methods in Enzymology , vol.176 , pp. 279-311
    • Rao, B.D.1
  • 276
    • 3242878900 scopus 로고    scopus 로고
    • Using nuclear magnetic resonance spectroscopy to study molten globule states of proteins
    • REDFIELD, C. (2004). Using nuclear magnetic resonance spectroscopy to study molten globule states of proteins. Methods 34, 121-132.
    • (2004) Methods , vol.34 , pp. 121-132
    • Redfield, C.1
  • 277
    • 0023705432 scopus 로고
    • Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR
    • RODER, H., ELOVE, G.A. & ENGLANDER, S.W. (1988). Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR. Nature 335, 700-704.
    • (1988) Nature , vol.335 , pp. 700-704
    • Roder, H.1    Elove, G.A.2    Englander, S.W.3
  • 278
    • 14544292475 scopus 로고    scopus 로고
    • NMR structure of Mistic, a membrane-integrating protein for membrane protein expression
    • ROOSILD, T. P., GREENWALD, J., VEGA, M., CASTRONOVO, S., RIEK, R. & CHOE, S. (2005). NMR structure of Mistic, a membrane-integrating protein for membrane protein expression. Science 307, 1317-1321.
    • (2005) Science , vol.307 , pp. 1317-1321
    • Roosild, T.P.1    Greenwald, J.2    Vega, M.3    Castronovo, S.4    Riek, R.5    Choe, S.6
  • 281
    • 37849015942 scopus 로고    scopus 로고
    • High-resolution structure determination of the CylR2 homodimer using paramagnetic relaxation enhancement and structure-based prediction of molecular alignment
    • RUMPEL, S., BECKER, S. & ZWECKSTETTER, M. (2008). High-resolution structure determination of the CylR2 homodimer using paramagnetic relaxation enhancement and structure-based prediction of molecular alignment. Journal of Biomolecular NMR 40, 1-13.
    • (2008) Journal of Biomolecular NMR , vol.40 , pp. 1-13
    • Rumpel, S.1    Becker, S.2    Zweckstetter, M.3
  • 282
    • 77649179384 scopus 로고    scopus 로고
    • Methyl groups as probes of supra-molecular structure, dynamics and function
    • RUSCHAK, A.M. & KAY, L. E. (2010). Methyl groups as probes of supra-molecular structure, dynamics and function. Journal of Biomolecular NMR 46, 75-87.
    • (2010) Journal of Biomolecular NMR , vol.46 , pp. 75-87
    • Ruschak, A.M.1    Kay, L.E.2
  • 284
    • 35848970780 scopus 로고    scopus 로고
    • TROSY-based z-exchange spectroscopy: Application to the determination of the activation energy for intermolecular protein translocation between specific sites on different DNA molecules
    • SAHU, D., CLORE, G.M. & IWAHARA, J. (2007). TROSY-based z-exchange spectroscopy: application to the determination of the activation energy for intermolecular protein translocation between specific sites on different DNA molecules. Journal of American Chemical Society 129, 13232-13237.
    • (2007) Journal of American Chemical Society , vol.129 , pp. 13232-13237
    • Sahu, D.1    Clore, G.M.2    Iwahara, J.3
  • 285
    • 17744364511 scopus 로고    scopus 로고
    • An NMR method for the determination of protein-binding interfaces using dioxygeninduced spin-lattice relaxation enhancement
    • SAKAKURA, M., NOBA, S., LUCHETTE, P. A., SHIMADA, I. & PROSSER, R. S. (2005). An NMR method for the determination of protein-binding interfaces using dioxygeninduced spin-lattice relaxation enhancement. Journal of American Chemical Society 127, 5826-5832.
    • (2005) Journal of American Chemical Society , vol.127 , pp. 5826-5832
    • Sakakura, M.1    Noba, S.2    Luchette, P.A.3    Shimada, I.4    Prosser, R.S.5
  • 286
    • 20444393525 scopus 로고    scopus 로고
    • Very fast twodimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds
    • SCHANDA, P. & BRUTSCHER, B. (2005). Very fast twodimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds. Journal of American Chemical Society 127, 8014-8015.
    • (2005) Journal of American Chemical Society , vol.127 , pp. 8014-8015
    • Schanda, P.1    Brutscher, B.2
  • 287
    • 0021772469 scopus 로고
    • Distance measurements in spin-labeled lysozyme
    • SCHMIDT, P.G. & KUNTZ, I. D. (1984). Distance measurements in spin-labeled lysozyme. Biochemistry 23, 4261-4266.
    • (1984) Biochemistry , vol.23 , pp. 4261-4266
    • Schmidt, P.G.1    Kuntz, I.D.2
  • 288
    • 0003337368 scopus 로고
    • One- and twodimensional NMR studies of exchanging amide protons in glutathione
    • SCHWARTZ, A.L. & CUTNELL, J. D. (1983). One- and twodimensional NMR studies of exchanging amide protons in glutathione. Journal of Magnetic Resonance 53, 398-411.
    • (1983) Journal of Magnetic Resonance , vol.53 , pp. 398-411
    • Schwartz, A.L.1    Cutnell, J.D.2
  • 289
    • 0035742163 scopus 로고    scopus 로고
    • The VMD-XPLOR visualization package for NMR structure refinement
    • SCHWIETERS, C.D. & CLORE, G.M. (2001). The VMD-XPLOR visualization package for NMR structure refinement. Journal of Magnetic Resonance 149, 239-244.
    • (2001) Journal of Magnetic Resonance , vol.149 , pp. 239-244
    • Schwieters, C.D.1    Clore, G.M.2
  • 290
    • 0036367763 scopus 로고    scopus 로고
    • Reweighted atomic densities to represent ensembles of NMR structures
    • SCHWIETERS, C.D. & CLORE, G.M. (2002). Reweighted atomic densities to represent ensembles of NMR structures. Journal of Biomolecular NMR 23, 221-225.
    • (2002) Journal of Biomolecular NMR , vol.23 , pp. 221-225
    • Schwieters, C.D.1    Clore, G.M.2
  • 293
    • 0024507697 scopus 로고
    • Structural characterization of the interactions between calmodulin and skeletal muscle myosin light chain kinase: Effect of peptide (576-594)G binding on the Ca2+-binding domains
    • SEEHOLZER, S.H. & WAND, A. J. (1989). Structural characterization of the interactions between calmodulin and skeletal muscle myosin light chain kinase: effect of peptide (576-594)G binding on the Ca2+-binding domains. Biochemistry 28, 4011-4020.
    • (1989) Biochemistry , vol.28 , pp. 4011-4020
    • Seeholzer, S.H.1    Wand, A.J.2
  • 294
    • 84881450365 scopus 로고    scopus 로고
    • NMR paves the way for atomic level descriptions of sparsely populated, transiently formed biomolecular conformers
    • SEKHAR, A. & KAY, L. E. (2013). NMR paves the way for atomic level descriptions of sparsely populated, transiently formed biomolecular conformers. Proceedings of the National Academy of Sciences of the United States of America 110, 12867-12874.
    • (2013) Proceedings of the National Academy of Sciences of the United States of America , vol.110 , pp. 12867-12874
    • Sekhar, A.1    Kay, L.E.2
  • 296
    • 84860258939 scopus 로고    scopus 로고
    • Protein fold determined by paramagnetic magic-angle spinning solid-state NMR spectroscopy
    • SENGUPTA, I., NADAUD, P. S., HELMUS, J. J., SCHWIETERS, C.D. & JARONIEC, C. P. (2012). Protein fold determined by paramagnetic magic-angle spinning solid-state NMR spectroscopy. Nature Chemistry 4, 410-417.
    • (2012) Nature Chemistry , vol.4 , pp. 410-417
    • Sengupta, I.1    Nadaud, P.S.2    Helmus, J.J.3    Schwieters, C.D.4    Jaroniec, C.P.5
  • 297
    • 84884248493 scopus 로고    scopus 로고
    • Protein structure determination with paramagnetic solidstate NMR spectroscopy
    • SENGUPTA, I., NADAUD, P.S. & JARONIEC, C. P. (2013). Protein structure determination with paramagnetic solidstate NMR spectroscopy. Accounts of Chemical Research 46, 2117-2126.
    • (2013) Accounts of Chemical Research , vol.46 , pp. 2117-2126
    • Sengupta, I.1    Nadaud, P.S.2    Jaroniec, C.P.3
  • 298
    • 84880132018 scopus 로고    scopus 로고
    • Protein backbone and sidechain torsion angles predicted from NMR chemical shifts using artificial neural networks
    • SHEN, Y. & BAX, A. (2013). Protein backbone and sidechain torsion angles predicted from NMR chemical shifts using artificial neural networks. Journal of Biomolecular NMR 56, 227-241.
    • (2013) Journal of Biomolecular NMR , vol.56 , pp. 227-241
    • Shen, Y.1    Bax, A.2
  • 300
    • 58149468410 scopus 로고    scopus 로고
    • De novo protein structure generation from incomplete chemical shift assignments
    • SHEN, Y., VERNON, R., BAKER, D. & BAX, A. (2009). De novo protein structure generation from incomplete chemical shift assignments. Journal of Biomolecular NMR 43, 63-78.
    • (2009) Journal of Biomolecular NMR , vol.43 , pp. 63-78
    • Shen, Y.1    Vernon, R.2    Baker, D.3    Bax, A.4
  • 303
    • 84876351687 scopus 로고    scopus 로고
    • Average conformations determined from PRE data provide high-resolution maps of transient tertiary interactions in disordered proteins
    • SILVESTRE-RYAN, J., BERTONCINI, C.W., FENWICK, R. B., ESTEBAN-MARTIN, S. & SALVATELLA, X. (2013). Average conformations determined from PRE data provide high-resolution maps of transient tertiary interactions in disordered proteins. Biophysical Journal 104, 1740-1751.
    • (2013) Biophysical Journal , vol.104 , pp. 1740-1751
    • Silvestre-Ryan, J.1    Bertoncini, C.W.2    Fenwick, R.B.3    Esteban-Martin, S.4    Salvatella, X.5
  • 304
    • 0037120879 scopus 로고    scopus 로고
    • Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments
    • SKRYNNIKOV, N. R., DAHLQUIST, F.W. & KAY, L. E. (2002). Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments. Journal of American Chemical Society 124, 12352-12360.
    • (2002) Journal of American Chemical Society , vol.124 , pp. 12352-12360
    • Skrynnikov, N.R.1    Dahlquist, F.W.2    Kay, L.E.3
  • 305
    • 36149008265 scopus 로고
    • Relaxation processes in a system of two spins
    • SOLOMON, I. (1955). Relaxation processes in a system of two spins. Physics Reviews 99, 559-565.
    • (1955) Physics Reviews , vol.99 , pp. 559-565
    • Solomon, I.1
  • 306
    • 36849133491 scopus 로고
    • Nuclear magnetic interactions in the HF molecule
    • SOLOMON, I. & BLOEMBERGEN, N. (1956). Nuclear magnetic interactions in the HF molecule. Journal of Chemical Physics 25, 261-266.
    • (1956) Journal of Chemical Physics , vol.25 , pp. 261-266
    • Solomon, I.1    Bloembergen, N.2
  • 308
    • 0026192276 scopus 로고
    • Measurement of the exchange rates of rapidly exchanging amide protons: Application to the study of calmodulin and its complex with a myosin light chain kinase fragment
    • SPERA, S., IKURA, M. & BAX, A. (1991). Measurement of the exchange rates of rapidly exchanging amide protons: application to the study of calmodulin and its complex with a myosin light chain kinase fragment. Journal of Biomolecular NMR 1, 155-165.
    • (1991) Journal of Biomolecular NMR , vol.1 , pp. 155-165
    • Spera, S.1    Ikura, M.2    Bax, A.3
  • 309
    • 33846928691 scopus 로고    scopus 로고
    • Quantitative dynamics and binding studies of the 20S proteasome by NMR
    • SPRANGERS, R. & KAY, L. E. (2007). Quantitative dynamics and binding studies of the 20S proteasome by NMR. Nature 445, 618-622.
    • (2007) Nature , vol.445 , pp. 618-622
    • Sprangers, R.1    Kay, L.E.2
  • 311
    • 34250821717 scopus 로고    scopus 로고
    • Mechanism of coupled folding and binding of an intrinsically disordered protein
    • SUGASE, K., DYSON, H.J. & WRIGHT, P. E. (2007). Mechanism of coupled folding and binding of an intrinsically disordered protein. Nature 447, 1021-1025.
    • (2007) Nature , vol.447 , pp. 1021-1025
    • Sugase, K.1    Dyson, H.J.2    Wright, P.E.3
  • 312
    • 36849135646 scopus 로고
    • NMR-relaxation mechanisms of O17 in aqueous solutions of paramagnetic cations and lifetime of water molecules in first coordination sphere
    • SWIFT, T.J. & CONNICK, R. E. (1962). NMR-relaxation mechanisms of O17 in aqueous solutions of paramagnetic cations and lifetime of water molecules in first coordination sphere. Journal of Chemical Physics 37, 307-320.
    • (1962) Journal of Chemical Physics , vol.37 , pp. 307-320
    • Swift, T.J.1    Connick, R.E.2
  • 313
    • 79959360942 scopus 로고    scopus 로고
    • Intra- and intermolecular translocation of the bi-domain transcription factor Oct1 characterized by liquid crystal and paramagnetic NMR
    • TAKAYAMA, Y. & CLORE, G.M. (2011). Intra- and intermolecular translocation of the bi-domain transcription factor Oct1 characterized by liquid crystal and paramagnetic NMR. Proceedings of the National Academy of Sciences of the United States of America 108, E169-E176.
    • (2011) Proceedings of the National Academy of Sciences of the United States of America , vol.108 , pp. E169-E176
    • Takayama, Y.1    Clore, G.M.2
  • 314
    • 84860359548 scopus 로고    scopus 로고
    • Interplay between minor and major groove-binding transcription factors Sox2 and Oct1 in translocation on DNA studied by paramagnetic and diamagnetic NMR
    • TAKAYAMA, Y. & CLORE, G.M. (2012). Interplay between minor and major groove-binding transcription factors Sox2 and Oct1 in translocation on DNA studied by paramagnetic and diamagnetic NMR. Journal of Biological Chemistry 287, 14349-14363.
    • (2012) Journal of Biological Chemistry , vol.287 , pp. 14349-14363
    • Takayama, Y.1    Clore, G.M.2
  • 315
    • 41149167049 scopus 로고    scopus 로고
    • Visualization of transient ultra-weak protein selfassociation in solution using paramagnetic relaxation enhancement
    • TANG, C., GHIRLANDO, R. & CLORE, G.M. (2008a). Visualization of transient ultra-weak protein selfassociation in solution using paramagnetic relaxation enhancement. Journal of American Chemical Society 130, 4048-4056.
    • (2008) Journal of American Chemical Society , vol.130 , pp. 4048-4056
    • Tang, C.1    Ghirlando, R.2    Clore, G.M.3
  • 316
    • 33751086423 scopus 로고    scopus 로고
    • Visualization of transient encounter complexes in protein-protein association
    • TANG, C., IWAHARA, J. & CLORE, G.M. (2006). Visualization of transient encounter complexes in protein-protein association. Nature 444, 383-386.
    • (2006) Nature , vol.444 , pp. 383-386
    • Tang, C.1    Iwahara, J.2    Clore, G.M.3
  • 317
    • 53349152834 scopus 로고    scopus 로고
    • Visualizing transient events in amino-terminal autoprocessing of HIV-1 protease
    • TANG, C., LOUIS, J. M., ANIANA, A., SUH, J.Y. & CLORE, G.M. (2008b). Visualizing transient events in amino-terminal autoprocessing of HIV-1 protease. Nature 455, 693-696.
    • (2008) Nature , vol.455 , pp. 693-696
    • Tang, C.1    Louis, J.M.2    Aniana, A.3    Suh, J.Y.4    Clore, G.M.5
  • 318
    • 35548976322 scopus 로고    scopus 로고
    • Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR
    • TANG, C., SCHWIETERS, C.D. & CLORE, G.M. (2007). Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR. Nature 449, 1078-1082.
    • (2007) Nature , vol.449 , pp. 1078-1082
    • Tang, C.1    Schwieters, C.D.2    Clore, G.M.3
  • 320
    • 0034132563 scopus 로고    scopus 로고
    • Direct refi nement against proton-proton dipolar couplings in NMR structure determination of macromolecules
    • TJANDRA, N., MARQUARDT, J. & CLORE, G.M. (2000). Direct refi nement against proton-proton dipolar couplings in NMR structure determination of macromolecules. Journal of Magnetic Resonance 142, 393-396.
    • (2000) Journal of Magnetic Resonance , vol.142 , pp. 393-396
    • Tjandra, N.1    Marquardt, J.2    Clore, G.M.3
  • 321
    • 0024809884 scopus 로고
    • Site-directed mutagenesis of colicin-E1 provides specific attachment sites for spin labels whose spectra are sensitive to local conformation
    • TODD, A. P., CONG, J. P., LEVINTHAL, F., LEVINTHAL, C. & HUBBELL, W. L. (1989). Site-directed mutagenesis of colicin-E1 provides specific attachment sites for spin labels whose spectra are sensitive to local conformation. Proteins 6, 294-305.
    • (1989) Proteins , vol.6 , pp. 294-305
    • Todd, A.P.1    Cong, J.P.2    Levinthal, F.3    Levinthal, C.4    Hubbell, W.L.5
  • 322
    • 84877846721 scopus 로고    scopus 로고
    • Structure and dynamics of an imidazoline nitroxide side chain with strongly hindered internal motion in proteins
    • TOLEDO WARSHAVIAK, D., KHRAMTSOV, V. V., CASCIO, D., ALTENBACH, C. & HUBBELL, W. L. (2013). Structure and dynamics of an imidazoline nitroxide side chain with strongly hindered internal motion in proteins. Journal of Magnetic Resonance 232, 53-61.
    • (2013) Journal of Magnetic Resonance , vol.232 , pp. 53-61
    • Toledo Warshaviak, D.1    Khramtsov, V.V.2    Cascio, D.3    Altenbach, C.4    Hubbell, W.L.5
  • 323
    • 0026750290 scopus 로고
    • The solution structures of calmodulin and its complexes with synthetic peptides based on target enzyme binding domains
    • TREWHELLA, J. (1992). The solution structures of calmodulin and its complexes with synthetic peptides based on target enzyme binding domains. Cell Calcium 13, 377-390.
    • (1992) Cell Calcium , vol.13 , pp. 377-390
    • Trewhella, J.1
  • 324
    • 4243179124 scopus 로고    scopus 로고
    • Theoretical study of R-1p rotating-frame and R-2 free-precession relaxation in the presence of n-site chemical exchange
    • TROTT, O. & PALMER, A. G. (2004). Theoretical study of R-1p rotating-frame and R-2 free-precession relaxation in the presence of n-site chemical exchange. Journal of Magnetic Resonance 170, 104-112.
    • (2004) Journal of Magnetic Resonance , vol.170 , pp. 104-112
    • Trott, O.1    Palmer, A.G.2
  • 325
    • 0041930989 scopus 로고    scopus 로고
    • Cross-correlated relaxation enhanced H-1-C-13 NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes
    • TUGARINOV, V., HWANG, P. M., OLLERENSHAW, J.E. & KAY, L. E. (2003). Cross-correlated relaxation enhanced H-1-C-13 NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes. Journal of American Chemical Society 125, 10420-10428.
    • (2003) Journal of American Chemical Society , vol.125 , pp. 10420-10428
    • Tugarinov, V.1    Hwang, P.M.2    Ollerenshaw, J.E.3    Kay, L.E.4
  • 326
    • 34547687784 scopus 로고    scopus 로고
    • Isotope labeling strategies for the study of high-molecular-weight proteins by solution NMR spectroscopy
    • TUGARINOV, V., KANELIS, V. & KAY, L. E. (2006). Isotope labeling strategies for the study of high-molecular-weight proteins by solution NMR spectroscopy. Nature Protocols 1, 749-754.
    • (2006) Nature Protocols , vol.1 , pp. 749-754
    • Tugarinov, V.1    Kanelis, V.2    Kay, L.E.3
  • 328
    • 0023758305 scopus 로고
    • NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A
    • UDGAONKAR, J.B. & BALDWIN, R. L. (1988). NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A. Nature 335, 694-699.
    • (1988) Nature , vol.335 , pp. 694-699
    • Udgaonkar, J.B.1    Baldwin, R.L.2
  • 330
    • 83455169144 scopus 로고    scopus 로고
    • Increasing the exchange time-scale that can be probed by CPMG relaxation dispersion NMR
    • VALLURUPALLI, P., BOUVIGNIES, G. & KAY, L. E. (2011). Increasing the exchange time-scale that can be probed by CPMG relaxation dispersion NMR. Journal of Physical Chemistry B 115, 14891-14900.
    • (2011) Journal of Physical Chemistry B , vol.115 , pp. 14891-14900
    • Vallurupalli, P.1    Bouvignies, G.2    Kay, L.E.3
  • 331
    • 84862061967 scopus 로고    scopus 로고
    • Studying "invisible" excited protein states in slow exchange with a major state conformation
    • VALLURUPALLI, P., BOUVIGNIES, G. & KAY, L. E. (2012). Studying "invisible" excited protein states in slow exchange with a major state conformation. Journal of American Chemical Society 134, 8148-8161.
    • (2012) Journal of American Chemical Society , vol.134 , pp. 8148-8161
    • Vallurupalli, P.1    Bouvignies, G.2    Kay, L.E.3
  • 332
    • 84884699481 scopus 로고    scopus 로고
    • A computational study of the effects of (13) C-(13) C scalar couplings on (13) C CEST NMR spectra: Towards studies on a uniformly (13) C-labeled protein
    • VALLURUPALLI, P., BOUVIGNIES, G. & KAY, L. E. (2013). A computational study of the effects of (13) C-(13) C scalar couplings on (13) C CEST NMR spectra: towards studies on a uniformly (13) C-labeled protein. Chembiochem 14, 1709-1713.
    • (2013) Chembiochem , vol.14 , pp. 1709-1713
    • Vallurupalli, P.1    Bouvignies, G.2    Kay, L.E.3
  • 333
    • 40949113653 scopus 로고    scopus 로고
    • Probing structure in invisible protein states with anisotropic NMR chemical shifts
    • VALLURUPALLI, P., HANSEN, D.F. & KAY, L. E. (2008a). Probing structure in invisible protein states with anisotropic NMR chemical shifts. Journal of American Chemical Society 130, 2734-2735.
    • (2008) Journal of American Chemical Society , vol.130 , pp. 2734-2735
    • Vallurupalli, P.1    Hansen, D.F.2    Kay, L.E.3
  • 336
    • 33747049527 scopus 로고    scopus 로고
    • Complementarity of ensemble and single-molecule measures of protein motion: A relaxation dispersion NMR study of an enzyme complex
    • VALLURUPALLI, P. &KAY, L. E. (2006). Complementarity of ensemble and single-molecule measures of protein motion: a relaxation dispersion NMR study of an enzyme complex. Proceedings of the National Academy of Sciences of the United States of America 103, 11910-11915.
    • (2006) Proceedings of the National Academy of Sciences of the United States of America , vol.103 , pp. 11910-11915
    • Vallurupalli, P.1    Kay, L.E.2
  • 337
    • 84875822105 scopus 로고    scopus 로고
    • Probing slow chemical exchange at carbonyl sites in proteins by chemical exchange saturation transfer NMR spectroscopy
    • VALLURUPALLI, P. & KAY, L. E. (2013). Probing slow chemical exchange at carbonyl sites in proteins by chemical exchange saturation transfer NMR spectroscopy. Angewandte Chemie International Edition English 52, 4156-4159.
    • (2013) Angewandte Chemie International Edition English , vol.52 , pp. 4156-4159
    • Vallurupalli, P.1    Kay, L.E.2
  • 339
    • 79952782590 scopus 로고    scopus 로고
    • Chemical exchange saturation transfer (CEST): What is in a name and what isn't?
    • VAN ZIJL, P.C. & YADAV, N. N. (2011). Chemical exchange saturation transfer (CEST): what is in a name and what isn't? Magnetic Resonance in Medicines 65, 927-948.
    • (2011) Magnetic Resonance in Medicines , vol.65 , pp. 927-948
    • Van Zijl, P.C.1    Yadav, N.N.2
  • 340
    • 0034070741 scopus 로고    scopus 로고
    • The NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein
    • VARANI, L., GUNDERSON, S. I., MATTAJ, I.W., KAY, L. E., NEUHAUS, D. & VARANI, G. (2000). The NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein. Nature Structural Biology 7, 329-335.
    • (2000) Nature Structural Biology , vol.7 , pp. 329-335
    • Varani, L.1    Gunderson, S.I.2    Mattaj, I.W.3    Kay, L.E.4    Neuhaus, D.5    Varani, G.6
  • 341
    • 80755190088 scopus 로고    scopus 로고
    • Automated sequence- and stereo-specific assignment of methyl-labeled proteins by paramagnetic relaxation and methyl-methyl nuclear Overhauser enhancement spectroscopy
    • VENDITTI, V., FAWZI, N.L. & CLORE, G.M. (2011). Automated sequence- and stereo-specific assignment of methyl-labeled proteins by paramagnetic relaxation and methyl-methyl nuclear Overhauser enhancement spectroscopy. Journal of Biomolecular NMR 51, 319-328.
    • (2011) Journal of Biomolecular NMR , vol.51 , pp. 319-328
    • Venditti, V.1    Fawzi, N.L.2    Clore, G.M.3
  • 342
    • 84863083642 scopus 로고    scopus 로고
    • An efficient protocol for incorporation of an unnatural amino acid in perdeuterated recombinant proteins using glucose-based media
    • VENDITTI, V., FAWZI, N.L. & CLORE, G.M. (2012). An efficient protocol for incorporation of an unnatural amino acid in perdeuterated recombinant proteins using glucose-based media. Journal of Biomolecular NMR 52, 191-195.
    • (2012) Journal of Biomolecular NMR , vol.52 , pp. 191-195
    • Venditti, V.1    Fawzi, N.L.2    Clore, G.M.3
  • 344
    • 84875224770 scopus 로고    scopus 로고
    • CEST: From basic principles to applications, challenges and opportunities
    • VINOGRADOV, E., SHERRY, A.D. & LENKINSKI, R. E. (2013). CEST: from basic principles to applications, challenges and opportunities. Journal of Magnetic Resonance 229, 155-172.
    • (2013) Journal of Magnetic Resonance , vol.229 , pp. 155-172
    • Vinogradov, E.1    Sherry, A.D.2    Lenkinski, R.E.3
  • 345
    • 34247210096 scopus 로고    scopus 로고
    • Identifying long-range structure in the intrinsically unstructured transactivation domain of p53
    • VISE, P., BARAL, B., STANCIK, A., LOWRY, D.F. & DAUGHDRILL, G.W. (2007). Identifying long-range structure in the intrinsically unstructured transactivation domain of p53. Proteins 67, 526-530.
    • (2007) Proteins , vol.67 , pp. 526-530
    • Vise, P.1    Baral, B.2    Stancik, A.3    Lowry, D.F.4    Daughdrill, G.W.5
  • 347
    • 78651327177 scopus 로고    scopus 로고
    • Mapping the encounter state of a transient protein complex by PRE NMR spectroscopy
    • VOLKOV, A. N., UBBINK, M. & VAN NULAND, N.A.J. (2010). Mapping the encounter state of a transient protein complex by PRE NMR spectroscopy. Journal of Biomolecular NMR 48, 225-236.
    • (2010) Journal of Biomolecular NMR , vol.48 , pp. 225-236
    • Volkov, A.N.1    Ubbink, M.2    Van Nuland, N.A.J.3
  • 349
    • 0020483829 scopus 로고
    • Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with twodimensional nuclear magnetic resonance
    • WAGNER, G. & WUTHRICH, K. (1982). Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with twodimensional nuclear magnetic resonance. Journal of Molecular Biology 160, 343-361.
    • (1982) Journal of Molecular Biology , vol.160 , pp. 343-361
    • Wagner, G.1    Wuthrich, K.2
  • 350
    • 34248190279 scopus 로고    scopus 로고
    • A beta oligomers - A decade of discovery
    • WALSH, D.M. & SELKOE, D. J. (2007). A beta oligomers - a decade of discovery. Journal of Neurochemistry 101, 1172-1184.
    • (2007) Journal of Neurochemistry , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 352
    • 0035917812 scopus 로고    scopus 로고
    • Expanding the genetic code of Escherichia coli
    • WANG, L., BROCK, A., HERBERICH, B. & SCHULTZ, P.G. (2001). Expanding the genetic code of Escherichia coli. Science 292, 498-500.
    • (2001) Science , vol.292 , pp. 498-500
    • Wang, L.1    Brock, A.2    Herberich, B.3    Schultz, P.G.4
  • 354
    • 0034145982 scopus 로고    scopus 로고
    • A new class of contrast agents for MRI based on proton chemical exchange dependent saturation transfer (CEST)
    • WARD, K. M., ALETRAS, A.H. & BALABAN, R. S. (2000). A new class of contrast agents for MRI based on proton chemical exchange dependent saturation transfer (CEST). Journal of Magnetic Resonance 143, 79-87.
    • (2000) Journal of Magnetic Resonance , vol.143 , pp. 79-87
    • Ward, K.M.1    Aletras, A.H.2    Balaban, R.S.3
  • 357
    • 33846636757 scopus 로고    scopus 로고
    • Sensitivity enhancement in (13)C solid-state NMR of protein microcrystals by use of paramagnetic metal ions for optimizing (1)H T(1) relaxation
    • WICKRAMASINGHE, N. P., KOTECHA, M., SAMOSON, A., PAST, J. & ISHII, Y. (2007). Sensitivity enhancement in (13)C solid-state NMR of protein microcrystals by use of paramagnetic metal ions for optimizing (1)H T(1) relaxation. Journal of Magnetic Resonance 184, 350-356.
    • (2007) Journal of Magnetic Resonance , vol.184 , pp. 350-356
    • Wickramasinghe, N.P.1    Kotecha, M.2    Samoson, A.3    Past, J.4    Ishii, Y.5
  • 358
    • 0001882103 scopus 로고
    • Studies of slow conformational equilibria in macromolecules by exchange of heteronuclear longitudinal 2-spin-order in a 2D difference correlation experiment
    • WIDER, G., NERI, D. & WUTHRICH, K. (1991). Studies of slow conformational equilibria in macromolecules by exchange of heteronuclear longitudinal 2-spin-order in a 2D difference correlation experiment. Journal of Biomolecular NMR 1, 93-98.
    • (1991) Journal of Biomolecular NMR , vol.1 , pp. 93-98
    • Wider, G.1    Neri, D.2    Wuthrich, K.3
  • 359
    • 36849135534 scopus 로고
    • Spin relaxation processes in a two-proton system undergoing anisotropic reorientation
    • WOESSNER, D. E. (1962). Spin relaxation processes in a two-proton system undergoing anisotropic reorientation. Journal of Chemical Physics 36, 1-4.
    • (1962) Journal of Chemical Physics , vol.36 , pp. 1-4
    • Woessner, D.E.1
  • 360
    • 0242299265 scopus 로고    scopus 로고
    • Protein alignment by a coexpressed lanthanide-binding tag for the measurement of residual dipolar couplings
    • WOHNERT, J., FRANZ, K. J., NITZ, M., IMPERIALI, B. & SCHWALBE, H. (2003). Protein alignment by a coexpressed lanthanide-binding tag for the measurement of residual dipolar couplings. Journal of American Chemical Society 125, 13338-13339.
    • (2003) Journal of American Chemical Society , vol.125 , pp. 13338-13339
    • Wohnert, J.1    Franz, K.J.2    Nitz, M.3    Imperiali, B.4    Schwalbe, H.5
  • 362
    • 33748557507 scopus 로고    scopus 로고
    • Recent successes of the energy landscape theory of protein folding and function
    • WOLYNES, P. G. (2005). Recent successes of the energy landscape theory of protein folding and function. Quarterly Review of Biophysics 38, 405-410.
    • (2005) Quarterly Review of Biophysics , vol.38 , pp. 405-410
    • Wolynes, P.G.1
  • 364
    • 84879184332 scopus 로고    scopus 로고
    • NMR relaxation in proteins with fast internal motions and slow conformational exchange: Model-free framework and Markov state simulations
    • XIA, J., DENG, N. J. & LEVY, R.M. (2013). NMR relaxation in proteins with fast internal motions and slow conformational exchange: model-free framework and Markov state simulations. Journal of Physical Chemistry B 117, 6625-6634.
    • (2013) Journal of Physical Chemistry B , vol.117 , pp. 6625-6634
    • Xia, J.1    Deng, N.J.2    Levy, R.M.3
  • 365
    • 1942496481 scopus 로고    scopus 로고
    • Calmodulin's flexibility allows for promiscuity in its interactions with target proteins and peptides
    • YAMNIUK, A.P. & VOGEL, H. J. (2004). Calmodulin's flexibility allows for promiscuity in its interactions with target proteins and peptides. Molecular Biotechnology 27, 33-57.
    • (2004) Molecular Biotechnology , vol.27 , pp. 33-57
    • Yamniuk, A.P.1    Vogel, H.J.2
  • 366
    • 1942457259 scopus 로고    scopus 로고
    • Conformational heterogeneity of an equilibrium folding intermediate quantified and mapped by scanning mutagenesis
    • YAN, S., GAWLAK, G., SMITH, J., SILVER, L., KOIDE, A. & KOIDE, S. (2004). Conformational heterogeneity of an equilibrium folding intermediate quantified and mapped by scanning mutagenesis. Journal of Molecular Biology 338, 811-825.
    • (2004) Journal of Molecular Biology , vol.338 , pp. 811-825
    • Yan, S.1    Gawlak, G.2    Smith, J.3    Silver, L.4    Koide, A.5    Koide, S.6
  • 367
    • 0036408312 scopus 로고    scopus 로고
    • Thermodynamic and kinetic exploration of the energy landscape of Borrelia burgdorferi OspA by native-state hydrogen exchange
    • YAN, S., KENNEDY, S.D. & KOIDE, S. (2002). Thermodynamic and kinetic exploration of the energy landscape of Borrelia burgdorferi OspA by native-state hydrogen exchange. Journal of Molecular Biology 323, 363-375.
    • (2002) Journal of Molecular Biology , vol.323 , pp. 363-375
    • Yan, S.1    Kennedy, S.D.2    Koide, S.3
  • 368
    • 0027529263 scopus 로고
    • Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation
    • ZHANG, Z. & SMITH, D. L. (1993). Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation. Protein Science 2, 522-531.
    • (1993) Protein Science , vol.2 , pp. 522-531
    • Zhang, Z.1    Smith, D.L.2
  • 369
    • 41949099222 scopus 로고    scopus 로고
    • Towards atomic resolution structural determination by single-particle cryo-electron microscopy
    • ZHOU, Z. H. (2008). Towards atomic resolution structural determination by single-particle cryo-electron microscopy. Current Opinion in Structural Biology 18, 218-228.
    • (2008) Current Opinion in Structural Biology , vol.18 , pp. 218-228
    • Zhou, Z.H.1
  • 370
    • 84885666400 scopus 로고    scopus 로고
    • NMR-based conformational ensembles explain pH-gated opening and closing of OmpG channel
    • ZHUANG, T., CHISHOLM, C., CHEN, M. & TAMM, L.K. (2013). NMR-based conformational ensembles explain pH-gated opening and closing of OmpG channel. Journal of American Chemical Society 135, 15101-15113.
    • (2013) Journal of American Chemical Society , vol.135 , pp. 15101-15113
    • Zhuang, T.1    Chisholm, C.2    Chen, M.3    Tamm, L.K.4


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