메뉴 건너뛰기




Volumn 57, Issue 3, 2013, Pages 263-280

Amplitudes and time scales of picosecond-to-microsecond motion in proteins studied by solid-state NMR: A critical evaluation of experimental approaches and application to crystalline ubiquitin

Author keywords

Dipolar couplings; Model free; Order parameters; Protein dynamics; REDOR; Relaxation; Solid state NMR; Ubiquitin

Indexed keywords

MICROCRYSTALLINE UBIQUITIN; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 84889826140     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-013-9787-x     Document Type: Article
Times cited : (65)

References (53)
  • 1
    • 57549117597 scopus 로고    scopus 로고
    • Protein side-chain dynamics as observed by solution- and solid-state NMR spectroscopy: A similarity revealed
    • 10.1021/ja804275p 10.1021/ja804275p
    • Agarwal V, Xue Y, Reif B, Skrynnikov N (2008) Protein side-chain dynamics as observed by solution- and solid-state NMR spectroscopy: a similarity revealed. J Am Chem Soc 130:16611-16621. doi: 10.1021/ja804275p
    • (2008) J Am Chem Soc , vol.130 , pp. 16611-16621
    • Agarwal, V.1    Xue, Y.2    Reif, B.3    Skrynnikov, N.4
  • 2
    • 84884242154 scopus 로고    scopus 로고
    • Proton-detected solid-state NMR spectroscopy at aliphatic sites: Application to crystalline systems
    • 130607095515005. doi: 10.1021/ar400063y
    • Asami S, Reif B (2013) Proton-detected solid-state NMR spectroscopy at aliphatic sites: application to crystalline systems. Acc Chem Res 130607095515005. doi: 10.1021/ar400063y
    • (2013) Acc Chem Res
    • Asami, S.1    Reif, B.2
  • 3
    • 78049369186 scopus 로고    scopus 로고
    • High resolution 1H-detected solid-state NMR spectroscopy of protein aliphatic resonances: Access to tertiary structure information
    • 10.1021/ja106170h 10.1021/ja106170h
    • Asami S, Schmieder P, Reif B (2010) High resolution 1H-detected solid-state NMR spectroscopy of protein aliphatic resonances: access to tertiary structure information. J Am Chem Soc 132:15133-15135. doi: 10.1021/ja106170h
    • (2010) J Am Chem Soc , vol.132 , pp. 15133-15135
    • Asami, S.1    Schmieder, P.2    Reif, B.3
  • 4
    • 81755177781 scopus 로고    scopus 로고
    • Kinetics of conformational sampling in ubiquitin
    • 10.1002/anie.201105086 10.1002/anie.201105086
    • Ban D, Funk M, Gulich R et al (2011) Kinetics of conformational sampling in ubiquitin. Angew Chem Int Ed Engl 50:11437-11440. doi: 10.1002/anie.201105086
    • (2011) Angew Chem Int Ed Engl , vol.50 , pp. 11437-11440
    • Ban, D.1    Funk, M.2    Gulich, R.3
  • 5
    • 1842862935 scopus 로고    scopus 로고
    • Anisotropic small amplitude peptide plane dynamics in proteins from residual dipolar couplings
    • 10.1021/Ja036977w 10.1021/ja036977w
    • Bernado P, Blackledge M (2004) Anisotropic small amplitude peptide plane dynamics in proteins from residual dipolar couplings. J Am Chem Soc 126:4907-4920. doi: 10.1021/Ja036977w
    • (2004) J Am Chem Soc , vol.126 , pp. 4907-4920
    • Bernado, P.1    Blackledge, M.2
  • 6
    • 0000411902 scopus 로고
    • NMR order parameters of biomolecules: A new analytical representation and application to the Gaussian Axial Fluctuation Model
    • 10.1021/ja00097a084
    • Brüschweiler R, Wright PE (1994) NMR order parameters of biomolecules: a new analytical representation and application to the Gaussian Axial Fluctuation Model. J Am Chem Soc 116:8426-8427
    • (1994) J Am Chem Soc , vol.116 , pp. 8426-8427
    • Brüschweiler, R.1    Wright, P.E.2
  • 7
    • 44649085834 scopus 로고    scopus 로고
    • TROSY effects in MAS solid-state NMR
    • 10.1002/Cmr.A.20106 10.1002/cmr.a.20106
    • Chevelkov V, Reif B (2008) TROSY effects in MAS solid-state NMR. Concepts Magn Reson Part A 32A:143-156. doi: 10.1002/Cmr.A.20106
    • (2008) Concepts Magn Reson Part A , vol.32 , pp. 143-156
    • Chevelkov, V.1    Reif, B.2
  • 8
    • 34548190759 scopus 로고    scopus 로고
    • Differential line broadening in MAS solid-state NMR due to dynamic interference
    • 10.1021/ja072024c 10.1021/ja072024c
    • Chevelkov V, Faelber K, Schrey A et al (2007) Differential line broadening in MAS solid-state NMR due to dynamic interference. J Am Chem Soc 129:10195-10200. doi: 10.1021/ja072024c
    • (2007) J Am Chem Soc , vol.129 , pp. 10195-10200
    • Chevelkov, V.1    Faelber, K.2    Schrey, A.3
  • 9
    • 41449113252 scopus 로고    scopus 로고
    • Measurement of 15 N-T1 relaxation rates in a perdeuterated protein by magic angle spinning solid-state nuclear magnetic resonance spectroscopy
    • 10.1063/1.2819311 2008JChPh.128e2316C 10.1063/1.2819311
    • Chevelkov V, Diehl A, Reif B (2008) Measurement of 15 N-T1 relaxation rates in a perdeuterated protein by magic angle spinning solid-state nuclear magnetic resonance spectroscopy. J Chem Phys 128:052316. doi: 10.1063/1.2819311
    • (2008) J Chem Phys , vol.128 , pp. 052316
    • Chevelkov, V.1    Diehl, A.2    Reif, B.3
  • 10
    • 69249213879 scopus 로고    scopus 로고
    • Quantitative analysis of backbone motion in proteins using MAS solid-state NMR spectroscopy
    • 10.1007/s10858-009-9348-5 10.1007/s10858-009-9348-5
    • Chevelkov V, Fink U, Reif B (2009a) Quantitative analysis of backbone motion in proteins using MAS solid-state NMR spectroscopy. J Biomol NMR 45:197-206. doi: 10.1007/s10858-009-9348-5
    • (2009) J Biomol NMR , vol.45 , pp. 197-206
    • Chevelkov, V.1    Fink, U.2    Reif, B.3
  • 11
    • 69249248134 scopus 로고    scopus 로고
    • Accurate determination of order parameters from H-1, N-15 dipolar couplings in MAS solid-state NMR experiments
    • 10.1021/ja902649u 10.1021/ja902649u
    • Chevelkov V, Fink U, Reif B (2009b) Accurate determination of order parameters from H-1, N-15 dipolar couplings in MAS solid-state NMR experiments. J Am Chem Soc 131:14018-14022. doi: 10.1021/ja902649u
    • (2009) J Am Chem Soc , vol.131 , pp. 14018-14022
    • Chevelkov, V.1    Fink, U.2    Reif, B.3
  • 12
    • 77950817927 scopus 로고    scopus 로고
    • Comparison of solid-state dipolar couplings and solution relaxation data provides insight into protein backbone dynamics
    • 10.1021/ja100645k 10.1021/ja100645k
    • Chevelkov V, Xue Y, Linser R et al (2010) Comparison of solid-state dipolar couplings and solution relaxation data provides insight into protein backbone dynamics. J Am Chem Soc 132:5015-5017. doi: 10.1021/ja100645k
    • (2010) J Am Chem Soc , vol.132 , pp. 5015-5017
    • Chevelkov, V.1    Xue, Y.2    Linser, R.3
  • 13
    • 0025046144 scopus 로고
    • Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins
    • 10.1021/ja00168a070
    • Clore GM, Szabo A, Bax A et al (1990) Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins. J Am Chem Soc 112:4989-4991
    • (1990) J Am Chem Soc , vol.112 , pp. 4989-4991
    • Clore, G.M.1    Szabo, A.2    Bax, A.3
  • 14
    • 0029400480 scopus 로고
    • NMRPIPE: A multidimensional spectral processing system based on Unix pipes
    • 10.1007/BF00197809
    • Delaglio F, Grzesiek S, Vuister G et al (1995) NMRPIPE: a multidimensional spectral processing system based on Unix pipes. J Biomol NMR 6:277-293
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.3
  • 15
    • 0042944212 scopus 로고    scopus 로고
    • Heteronuclear dipolar recoupling in liquid crystals and solids by PISEMA-type pulse sequences
    • 10.1016/S1090-7807(03)00180-0 2003JMagR.164.165D 10.1016/S1090-7807(03) 00180-0
    • Dvinskikh S, Zimmermann H, Maliniak A, Sandstrom D (2003) Heteronuclear dipolar recoupling in liquid crystals and solids by PISEMA-type pulse sequences. J Magn Reson 164:165-170. doi: 10.1016/S1090-7807(03)00180-0
    • (2003) J Magn Reson , vol.164 , pp. 165-170
    • Dvinskikh, S.1    Zimmermann, H.2    Maliniak, A.3    Sandstrom, D.4
  • 16
    • 70149102207 scopus 로고    scopus 로고
    • Accurate sampling of high-frequency motions in proteins by steady-state (15)N-{(1)H} nuclear Overhauser effect measurements in the presence of cross-correlated relaxation
    • 10.1021/ja809526q 10.1021/ja809526q
    • Ferrage F, Cowburn D, Ghose R (2009) Accurate sampling of high-frequency motions in proteins by steady-state (15)N-{(1)H} nuclear Overhauser effect measurements in the presence of cross-correlated relaxation. J Am Chem Soc 131:6048-6049. doi: 10.1021/ja809526q
    • (2009) J Am Chem Soc , vol.131 , pp. 6048-6049
    • Ferrage, F.1    Cowburn, D.2    Ghose, R.3
  • 17
    • 24644462659 scopus 로고    scopus 로고
    • Magic-angle spinning solid-state NMR spectroscopy of the beta 1 immunoglobulin binding domain of protein G (GB1): N-15 and C-13 chemical shift assignments and conformational analysis
    • 10.1021/ja044497e 10.1021/ja044497e
    • Franks W, Zhou D, Wylie B et al (2005) Magic-angle spinning solid-state NMR spectroscopy of the beta 1 immunoglobulin binding domain of protein G (GB1): N-15 and C-13 chemical shift assignments and conformational analysis. J Am Chem Soc 127:12291-12305. doi: 10.1021/ja044497e
    • (2005) J Am Chem Soc , vol.127 , pp. 12291-12305
    • Franks, W.1    Zhou, D.2    Wylie, B.3
  • 18
    • 34447503697 scopus 로고    scopus 로고
    • Conformational entropy in molecular recognition by proteins
    • 10.1038/Nature05959 2007Natur.448.325F 10.1038/nature05959
    • Frederick K, Marlow M, Valentine K, Wand A (2007) Conformational entropy in molecular recognition by proteins. Nature 448:325-329. doi: 10.1038/Nature05959
    • (2007) Nature , vol.448 , pp. 325-329
    • Frederick, K.1    Marlow, M.2    Valentine, K.3    Wand, A.4
  • 19
    • 4544369426 scopus 로고    scopus 로고
    • Site-specific backbone dynamics from a crystalline protein by solid-state NMR spectroscopy
    • 10.1021/ja046578g
    • Giraud N, Bockmann A, Lesage A et al (2004) Site-specific backbone dynamics from a crystalline protein by solid-state NMR spectroscopy. J Am Chem Soc 126:11422-11423
    • (2004) J Am Chem Soc , vol.126 , pp. 11422-11423
    • Giraud, N.1    Bockmann, A.2    Lesage, A.3
  • 20
    • 84876837158 scopus 로고    scopus 로고
    • Characterization of the free-energy landscapes of proteins by NMR-guided metadynamics
    • 10.1073/pnas.1218350110 2013PNAS.110.6817G 10.1073/pnas.1218350110
    • Granata D, Camilloni C, Vendruscolo M, Laio A (2013) Characterization of the free-energy landscapes of proteins by NMR-guided metadynamics. Proc Natl Acad Sci USA 110:6817-6822. doi: 10.1073/pnas.1218350110
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 6817-6822
    • Granata, D.1    Camilloni, C.2    Vendruscolo, M.3    Laio, A.4
  • 21
    • 85011817347 scopus 로고
    • Detection of weak heteronuclear dipolar coupling by rotational-echo double-resonance nuclear-magnetic-resonance
    • 10.1016/B978-0-12-025513-9.50009-4
    • Gullion T, Schaefer J (1989) Detection of weak heteronuclear dipolar coupling by rotational-echo double-resonance nuclear-magnetic-resonance. Adv Magn Reson 13(13):57-83
    • (1989) Adv Magn Reson , vol.13 , Issue.13 , pp. 57-83
    • Gullion, T.1    Schaefer, J.2
  • 22
    • 77749237271 scopus 로고    scopus 로고
    • Conformational flexibility of Y154Stop human prion protein amyloid fibrils probed by solid-state nuclear magnetic resonance spectroscopy
    • 10.1021/ja909827v 10.1021/ja909827v
    • Helmus J, Surewicz K, Surewicz W, Jaroniec C (2010) Conformational flexibility of Y154Stop human prion protein amyloid fibrils probed by solid-state nuclear magnetic resonance spectroscopy. J Am Chem Soc 132:2393-2403. doi: 10.1021/ja909827v
    • (2010) J Am Chem Soc , vol.132 , pp. 2393-2403
    • Helmus, J.1    Surewicz, K.2    Surewicz, W.3    Jaroniec, C.4
  • 23
    • 0034607459 scopus 로고    scopus 로고
    • Local structure and relaxation in solid-state NMR: Accurate measurement of amide N-H bond lengths and H-N-H bond angles
    • 10.1021/ja9913737
    • Hohwy M, Jaroniec C, Reif B et al (2000) Local structure and relaxation in solid-state NMR: accurate measurement of amide N-H bond lengths and H-N-H bond angles. J Am Chem Soc 122:3218-3219
    • (2000) J Am Chem Soc , vol.122 , pp. 3218-3219
    • Hohwy, M.1    Jaroniec, C.2    Reif, B.3
  • 24
    • 83055186903 scopus 로고    scopus 로고
    • 1H-13C/ 1H-15 N heteronuclear dipolar recoupling by R-Symmetry sequences under fast Magic Angle spinning for dynamics analysis of biological and organic solids
    • 10.1021/ja203771a 10.1021/ja203771a
    • Hou G, Byeon I-JL, Ahn J et al (2011) 1H-13C/ 1H-15 N heteronuclear dipolar recoupling by R-Symmetry sequences under fast Magic Angle spinning for dynamics analysis of biological and organic solids. J Am Chem Soc 133:18646-18655. doi: 10.1021/ja203771a
    • (2011) J Am Chem Soc , vol.133 , pp. 18646-18655
    • Hou, G.1    Byeon, I.-J.2    Ahn, J.3
  • 25
    • 84873844866 scopus 로고    scopus 로고
    • Multidimensional magic angle spinning NMR spectroscopy for site-resolved measurement of proton chemical shift anisotropy in biological solids
    • 10.1021/ja3084972 10.1021/ja3084972
    • Hou G, Paramasivam S, Yan S et al (2013) Multidimensional magic angle spinning NMR spectroscopy for site-resolved measurement of proton chemical shift anisotropy in biological solids. J Am Chem Soc 135:1358-1368. doi: 10.1021/ja3084972
    • (2013) J Am Chem Soc , vol.135 , pp. 1358-1368
    • Hou, G.1    Paramasivam, S.2    Yan, S.3
  • 26
    • 79958837339 scopus 로고    scopus 로고
    • An introduction to NMR-based approaches for measuring protein dynamics
    • 10.1016/j.bbapap.2010.10.012 10.1016/j.bbapap.2010.10.012
    • Kleckner IR, Foster MP (2011) An introduction to NMR-based approaches for measuring protein dynamics. BBA Proteins Proteomics 1814:942-968. doi: 10.1016/j.bbapap.2010.10.012
    • (2011) BBA Proteins Proteomics , vol.1814 , pp. 942-968
    • Kleckner, I.R.1    Foster, M.P.2
  • 27
    • 84863955843 scopus 로고    scopus 로고
    • Structure and backbone dynamics of a microcrystalline metalloprotein by solid-state NMR
    • 10.1073/pnas.1204515109
    • Knight MJ, Pell AJ, Bertini I et al (2012) Structure and backbone dynamics of a microcrystalline metalloprotein by solid-state NMR. Proc Natl Acad Sci USA. doi: 10.1073/pnas.1204515109
    • (2012) Proc Natl Acad Sci USA
    • Knight, M.J.1    Pell, A.J.2    Bertini, I.3
  • 28
    • 77956081825 scopus 로고    scopus 로고
    • Microsecond time scale mobility in a solid protein as studied by the 15 N R1ρSite-specific NMR relaxation rates
    • 10.1021/ja103582n 10.1021/ja103582n
    • Krushelnitsky A, Zinkevich T, Reichert D et al (2010) Microsecond time scale mobility in a solid protein as studied by the 15 N R1ρSite-specific NMR relaxation rates. J Am Chem Soc 132:11850-11853. doi: 10.1021/ja103582n
    • (2010) J Am Chem Soc , vol.132 , pp. 11850-11853
    • Krushelnitsky, A.1    Zinkevich, T.2    Reichert, D.3
  • 29
    • 46949093648 scopus 로고    scopus 로고
    • Self-consistent residual dipolar coupling based model-free analysis for the robust determination of nanosecond to microsecond protein dynamics
    • 10.1007/S10858-008-9244-4 10.1007/s10858-008-9244-4
    • Lakomek N, Walter K, Fares C et al (2008) Self-consistent residual dipolar coupling based model-free analysis for the robust determination of nanosecond to microsecond protein dynamics. J Biomol NMR 41:139-155. doi: 10.1007/S10858-008-9244-4
    • (2008) J Biomol NMR , vol.41 , pp. 139-155
    • Lakomek, N.1    Walter, K.2    Fares, C.3
  • 30
    • 0011352041 scopus 로고    scopus 로고
    • Symmetry-based pulse sequences in magic-angle spinning solid-state NMR
    • Levitt M (2002) Symmetry-based pulse sequences in magic-angle spinning solid-state NMR. Encycl Nucl Magn Reson 9:165-196
    • (2002) Encycl Nucl Magn Reson , vol.9 , pp. 165-196
    • Levitt, M.1
  • 31
    • 77950392888 scopus 로고    scopus 로고
    • Anisotropic collective motion contributes to nuclear spin relaxation in crystalline proteins
    • 10.1021/ja907067j 10.1021/ja907067j
    • Lewandowski JR, Sein J, Blackledge M, Emsley L (2010a) Anisotropic collective motion contributes to nuclear spin relaxation in crystalline proteins. J Am Chem Soc 132:1246-1248. doi: 10.1021/ja907067j
    • (2010) J Am Chem Soc , vol.132 , pp. 1246-1248
    • Lewandowski, J.R.1    Sein, J.2    Blackledge, M.3    Emsley, L.4
  • 32
    • 77953648918 scopus 로고    scopus 로고
    • Measurement of site-specific (13)C spin-lattice relaxation in a crystalline protein
    • 10.1021/ja102744b
    • Lewandowski JR, Sein J, Sass HJ et al (2010b) Measurement of site-specific (13)C spin-lattice relaxation in a crystalline protein. J Am Chem Soc. doi: 10.1021/ja102744b
    • (2010) J Am Chem Soc
    • Lewandowski, J.R.1    Sein, J.2    Sass, H.J.3
  • 33
    • 80054990767 scopus 로고    scopus 로고
    • Site-specific measurement of slow motions in proteins
    • 10.1021/ja206815h 10.1021/ja206815h
    • Lewandowski JR, Sass HJ, Grzesiek S et al (2011) Site-specific measurement of slow motions in proteins. J Am Chem Soc 133:16762-16765. doi: 10.1021/ja206815h
    • (2011) J Am Chem Soc , vol.133 , pp. 16762-16765
    • Lewandowski, J.R.1    Sass, H.J.2    Grzesiek, S.3
  • 34
    • 0032581920 scopus 로고    scopus 로고
    • Anisotropic intramolecular backbone dynamics of ubiquitin characterized by NMR relaxation and MD computer simulation
    • 10.1021/ja9810179
    • Lienin S, Bremi T, Brutscher B et al (1998) Anisotropic intramolecular backbone dynamics of ubiquitin characterized by NMR relaxation and MD computer simulation. J Am Chem Soc 120:9870-9879
    • (1998) J Am Chem Soc , vol.120 , pp. 9870-9879
    • Lienin, S.1    Bremi, T.2    Brutscher, B.3
  • 35
    • 18544370347 scopus 로고
    • Analysis of NMR relaxation data on macromolecules using the model-free approach
    • Lipari G, Szabo A (1982a) Analysis of NMR relaxation data on macromolecules using the model-free approach. Biophys J 37:A380-A380
    • (1982) Biophys J , vol.37
    • Lipari, G.1    Szabo, A.2
  • 36
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules. 1. Theory and range of validity
    • 10.1021/ja00381a009
    • Lipari G, Szabo A (1982b) Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules. 1. Theory and range of validity. J Am Chem Soc 104:4546-4559
    • (1982) J Am Chem Soc , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 37
    • 77953065253 scopus 로고    scopus 로고
    • Progress in nuclear magnetic resonance spectroscopy
    • 10.1016/j.pnmrs.2010.03.002 10.1016/j.pnmrs.2010.03.002
    • Meirovitch E, Shapiro YE, Polimeno A, Freed JH (2010) Progress in nuclear magnetic resonance spectroscopy. Prog Nucl Magn Reson Spectrosc 56:360-405. doi: 10.1016/j.pnmrs.2010.03.002
    • (2010) Prog Nucl Magn Reson Spectrosc , vol.56 , pp. 360-405
    • Meirovitch, E.1    Shapiro, Y.E.2    Polimeno, A.3    Freed, J.H.4
  • 38
    • 70449769332 scopus 로고    scopus 로고
    • Observing biological dynamics at atomic resolution using NMR
    • 10.1016/j.tibs.2009.07.004 10.1016/j.tibs.2009.07.004
    • Mittermaier AK, Kay LE (2009) Observing biological dynamics at atomic resolution using NMR. Trends Biochem Sci 34:601-611. doi: 10.1016/j.tibs.2009. 07.004
    • (2009) Trends Biochem Sci , vol.34 , pp. 601-611
    • Mittermaier, A.K.1    Kay, L.E.2
  • 39
    • 84870853885 scopus 로고    scopus 로고
    • Atomic-resolution structural dynamics in crystalline proteins from NMR and molecular simulation
    • doi: 10.1021/jz3016233
    • Mollica L, Baias M, Lewandowski JR et al (2012) Atomic-resolution structural dynamics in crystalline proteins from NMR and molecular simulation. J Phys Chem Letters 3657-3662. doi: 10.1021/jz3016233
    • (2012) J Phys Chem Letters , pp. 3657-3662
    • Mollica, L.1    Baias, M.2    Lewandowski, J.R.3    Al, E.4
  • 41
    • 33845557418 scopus 로고
    • Two-dimensional rotational spin-echo nuclear magnetic resonance in solids: Correlation of chemical shift and dipolar interactions
    • 10.1021/ja00400a007
    • Munowitz MG, Griffin RG, Bodenhausen G, Huang TH (1981) Two-dimensional rotational spin-echo nuclear magnetic resonance in solids: correlation of chemical shift and dipolar interactions. J Am Chem Soc 103:2529-2533
    • (1981) J Am Chem Soc , vol.103 , pp. 2529-2533
    • Munowitz, M.G.1    Griffin, R.G.2    Bodenhausen, G.3    Huang, T.H.4
  • 42
    • 4243155782 scopus 로고    scopus 로고
    • NMR characterization of the dynamics of biomacromolecules
    • 10.1021/Cr030413t 10.1021/cr030413t
    • Palmer AG (2004) NMR characterization of the dynamics of biomacromolecules. Chem Rev 104:3623-3640. doi: 10.1021/Cr030413t
    • (2004) Chem Rev , vol.104 , pp. 3623-3640
    • Palmer, A.G.1
  • 43
    • 0001913395 scopus 로고
    • On the theory of relaxation processes
    • 10.1147/rd.11.0019
    • Redfield AG (1957) On the theory of relaxation processes. IBM J Res Devel 1:19-31
    • (1957) IBM J Res Devel , vol.1 , pp. 19-31
    • Redfield, A.G.1
  • 44
    • 70349784868 scopus 로고    scopus 로고
    • Protein conformational flexibility from structure-free analysis of NMR dipolar couplings: Quantitative and absolute determination of backbone motion in ubiquitin
    • 10.1002/anie.200900476 10.1002/anie.200900476
    • Salmon L, Bouvignies G, Markwick P et al (2009) Protein conformational flexibility from structure-free analysis of NMR dipolar couplings: quantitative and absolute determination of backbone motion in ubiquitin. Angew Chem Int Edit 48:4154-4157. doi: 10.1002/anie.200900476
    • (2009) Angew Chem Int Edit , vol.48 , pp. 4154-4157
    • Salmon, L.1    Bouvignies, G.2    Markwick, P.3
  • 45
    • 72949090622 scopus 로고    scopus 로고
    • Direct detection of (3 h)J(NC') hydrogen-bond scalar couplings in proteins by solid-state NMR spectroscopy
    • 10.1002/anie.200904411 10.1002/anie.200904411
    • Schanda P, Huber M, Verel R et al (2009) Direct detection of (3 h)J(NC') hydrogen-bond scalar couplings in proteins by solid-state NMR spectroscopy. Angew Chem Int Ed Engl 48:9322-9325. doi: 10.1002/anie.200904411
    • (2009) Angew Chem Int Ed Engl , vol.48 , pp. 9322-9325
    • Schanda, P.1    Huber, M.2    Verel, R.3
  • 46
    • 78449258852 scopus 로고    scopus 로고
    • Quantitative analysis of protein backbone dynamics in microcrystalline ubiquitin by solid-state NMR spectroscopy
    • 10.1021/ja100726a 10.1021/ja100726a
    • Schanda P, Meier BH, Ernst M (2010) Quantitative analysis of protein backbone dynamics in microcrystalline ubiquitin by solid-state NMR spectroscopy. J Am Chem Soc 132:15957-15967. doi: 10.1021/ja100726a
    • (2010) J Am Chem Soc , vol.132 , pp. 15957-15967
    • Schanda, P.1    Meier, B.H.2    Ernst, M.3
  • 47
    • 80855144829 scopus 로고    scopus 로고
    • Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion
    • 10.1002/anie.201103944 10.1002/anie.201103944
    • Schanda P, Huber M, Boisbouvier J et al (2011a) Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion. Angew Chem Int Ed Engl 50:11005-11009. doi: 10.1002/anie.201103944
    • (2011) Angew Chem Int Ed Engl , vol.50 , pp. 11005-11009
    • Schanda, P.1    Huber, M.2    Boisbouvier, J.3
  • 48
    • 79955883734 scopus 로고    scopus 로고
    • Accurate measurement of one-bond H-X heteronuclear dipolar couplings in MAS solid-state NMR
    • 10.1016/j.jmr.2011.03.015 2011JMagR.210.246S 10.1016/j.jmr.2011.03.015
    • Schanda P, Meier BH, Ernst M (2011b) Accurate measurement of one-bond H-X heteronuclear dipolar couplings in MAS solid-state NMR. J Magn Reson 210:246-259. doi: 10.1016/j.jmr.2011.03.015
    • (2011) J Magn Reson , vol.210 , pp. 246-259
    • Schanda, P.1    Meier, B.H.2    Ernst, M.3
  • 49
    • 0001876029 scopus 로고
    • Computer simulations in magnetic resonance. An object-oriented programming approach
    • 1994JMagR.106.75S 10.1006/jmra.1994.1008
    • Smith S, Levante T, Meier B, Ernst R (1994) Computer simulations in magnetic resonance. An object-oriented programming approach. J Magn Reson 106:75-105
    • (1994) J Magn Reson , vol.106 , pp. 75-105
    • Smith, S.1    Levante, T.2    Meier, B.3    Ernst, R.4
  • 50
    • 84866359497 scopus 로고    scopus 로고
    • Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopy
    • 10.1021/ja303591y 10.1021/ja303591y
    • Tollinger M, Sivertsen AC, Meier BH et al (2012) Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopy. J Am Chem Soc 134:14800-14807. doi: 10.1021/ja303591y
    • (2012) J Am Chem Soc , vol.134 , pp. 14800-14807
    • Tollinger, M.1    Sivertsen, A.C.2    Meier, B.H.3
  • 51
    • 84856728860 scopus 로고    scopus 로고
    • μs time-scale conformational exchange in proteins: Using long MD trajectory to simulate NMR relaxation dispersion data
    • 10.1021/ja206442c
    • Xue Y, Ward JM, Yuwen T et al (2011) μs time-scale conformational exchange in proteins: using long MD trajectory to simulate NMR relaxation dispersion data. J Am Chem Soc. doi: 10.1021/ja206442c
    • (2011) J Am Chem Soc
    • Xue, Y.1    Ward, J.M.2    Yuwen, T.3
  • 52
    • 0030601792 scopus 로고    scopus 로고
    • Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: Application to protein folding
    • 10.1006/jmbi.1996.0581
    • Yang D, Kay L (1996) Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: application to protein folding. J Mol Biol 263:369-382
    • (1996) J Mol Biol , vol.263 , pp. 369-382
    • Yang, D.1    Kay, L.2
  • 53
    • 70349756880 scopus 로고    scopus 로고
    • Dynamics of reassembled thioredoxin studied by magic angle spinning NMR: Snapshots from different time scales
    • 10.1021/ja9037802 10.1021/ja9037802
    • Yang J, Tasayco M, Polenova T (2009) Dynamics of reassembled thioredoxin studied by magic angle spinning NMR: snapshots from different time scales. J Am Chem Soc 131:13690-13702. doi: 10.1021/ja9037802
    • (2009) J Am Chem Soc , vol.131 , pp. 13690-13702
    • Yang, J.1    Tasayco, M.2    Polenova, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.