메뉴 건너뛰기




Volumn 92, Issue , 2013, Pages 219-251

Protein functional dynamics in multiple timescales as studied by NMR spectroscopy

Author keywords

Enzyme kinetics; Functional dynamics; NMR spectroscopy; Protein allosterism

Indexed keywords

DIHYDROFOLATE REDUCTASE; ENZYME PRECURSOR; PERIPLASMIC BINDING PROTEIN; PROTEIN; PROTON; TRYPTOPHAN;

EID: 84896737712     PISSN: 18761623     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-411636-8.00006-7     Document Type: Chapter
Times cited : (18)

References (109)
  • 2
    • 33646943202 scopus 로고    scopus 로고
    • Molecular dynamics: Survey of methods for simulating the activity of proteins
    • S.A. Adcock, and J.A. McCammon Molecular dynamics: Survey of methods for simulating the activity of proteins Chemical Reviews 106 2006 1589 1615
    • (2006) Chemical Reviews , vol.106 , pp. 1589-1615
    • Adcock, S.A.1    McCammon, J.A.2
  • 3
    • 0036967268 scopus 로고    scopus 로고
    • Intramolecular dynamics of low molecular weight protein tyrosine phosphatase in monomer-dimer equilibrium studied by NMR: A model for changes in dynamics upon target binding
    • T. Akerud, E. Thulin, R.L. Van Etten, and M. Akke Intramolecular dynamics of low molecular weight protein tyrosine phosphatase in monomer-dimer equilibrium studied by NMR: A model for changes in dynamics upon target binding Journal of Molecular Biology 322 2002 137 152
    • (2002) Journal of Molecular Biology , vol.322 , pp. 137-152
    • Akerud, T.1    Thulin, E.2    Van Etten, R.L.3    Akke, M.4
  • 4
    • 84859332583 scopus 로고    scopus 로고
    • Conformational dynamics and thermodynamics of protein-ligand binding studied by NMR relaxation
    • M. Akke Conformational dynamics and thermodynamics of protein-ligand binding studied by NMR relaxation Biochemical Society Transactions 40 2012 419 423
    • (2012) Biochemical Society Transactions , vol.40 , pp. 419-423
    • Akke, M.1
  • 5
    • 0028945948 scopus 로고
    • Sugar recognition by a glucose/galactose receptor. Evaluation of binding energetics from molecular dynamics simulations
    • J. Aqvist, and S.L. Mowbray Sugar recognition by a glucose/galactose receptor. Evaluation of binding energetics from molecular dynamics simulations The Journal of Biological Chemistry 270 1995 9978 9981
    • (1995) The Journal of Biological Chemistry , vol.270 , pp. 9978-9981
    • Aqvist, J.1    Mowbray, S.L.2
  • 7
    • 77952938726 scopus 로고    scopus 로고
    • Global dynamics of proteins: Bridging between structure and function
    • I. Bahar, T.R. Lezon, L.W. Yang, and E. Eyal Global dynamics of proteins: Bridging between structure and function Annual Review of Biophysics 39 2010 23 42
    • (2010) Annual Review of Biophysics , vol.39 , pp. 23-42
    • Bahar, I.1    Lezon, T.R.2    Yang, L.W.3    Eyal, E.4
  • 8
    • 25844431698 scopus 로고    scopus 로고
    • Coarse-grained normal mode analysis in structural biology
    • I. Bahar, and A.J. Rader Coarse-grained normal mode analysis in structural biology Current Opinion in Structural Biology 15 2005 586 592
    • (2005) Current Opinion in Structural Biology , vol.15 , pp. 586-592
    • Bahar, I.1    Rader, A.J.2
  • 9
    • 77749286394 scopus 로고    scopus 로고
    • Ligand-free open-closed transitions of periplasmic binding proteins: The case of glutamine-binding protein
    • G.A. Bermejo, M.P. Strub, C. Ho, and N. Tjandra Ligand-free open-closed transitions of periplasmic binding proteins: The case of glutamine-binding protein Biochemistry 49 2010 1893 1902
    • (2010) Biochemistry , vol.49 , pp. 1893-1902
    • Bermejo, G.A.1    Strub, M.P.2    Ho, C.3    Tjandra, N.4
  • 10
    • 0346634883 scopus 로고    scopus 로고
    • Combined use of NMR relaxation measurements and hydrodynamic calculations to study protein association. Evidence for tetramers of low molecular weight protein tyrosine phosphatase in solution
    • P. Bernado, T. Akerud, J. Garcia de la Torre, M. Akke, and M. Pons Combined use of NMR relaxation measurements and hydrodynamic calculations to study protein association. Evidence for tetramers of low molecular weight protein tyrosine phosphatase in solution Journal of the American Chemical Society 125 2003 916 923
    • (2003) Journal of the American Chemical Society , vol.125 , pp. 916-923
    • Bernado, P.1    Akerud, T.2    Garcia De La Torre, J.3    Akke, M.4    Pons, M.5
  • 11
    • 0035996729 scopus 로고    scopus 로고
    • Interpretation of 15N NMR relaxation data of globular proteins using hydrodynamic calculations with HYDRONMR
    • P. Bernado, J. Garcia de la Torre, and M. Pons Interpretation of 15N NMR relaxation data of globular proteins using hydrodynamic calculations with HYDRONMR Journal of Biomolecular NMR 23 2002 139 150
    • (2002) Journal of Biomolecular NMR , vol.23 , pp. 139-150
    • Bernado, P.1    Garcia De La Torre, J.2    Pons, M.3
  • 13
    • 80855143648 scopus 로고    scopus 로고
    • Identification of endogenous ligands bound to bacterially expressed human and E. coli dihydrofolate reductase by 2D NMR
    • G. Bhabha, L. Tuttle, M.A. Martinez-Yamout, and P.E. Wright Identification of endogenous ligands bound to bacterially expressed human and E. coli dihydrofolate reductase by 2D NMR FEBS Letters 585 2011 3528 3532
    • (2011) FEBS Letters , vol.585 , pp. 3528-3532
    • Bhabha, G.1    Tuttle, L.2    Martinez-Yamout, M.A.3    Wright, P.E.4
  • 14
    • 0027057525 scopus 로고
    • Functional mapping of the surface of Escherichia coli ribose-binding protein: Mutations that affect chemotaxis and transport
    • R.A. Binnie, H. Zhang, S. Mowbray, and M.A. Hermodson Functional mapping of the surface of Escherichia coli ribose-binding protein: Mutations that affect chemotaxis and transport Protein Science 1 1992 1642 1651
    • (1992) Protein Science , vol.1 , pp. 1642-1651
    • Binnie, R.A.1    Zhang, H.2    Mowbray, S.3    Hermodson, M.A.4
  • 16
    • 0032511137 scopus 로고    scopus 로고
    • Multiple open forms of ribose-binding protein trace the path of its conformational change
    • A.J. Bjorkman, and S.L. Mowbray Multiple open forms of ribose-binding protein trace the path of its conformational change Journal of Molecular Biology 279 1998 651 664
    • (1998) Journal of Molecular Biology , vol.279 , pp. 651-664
    • Bjorkman, A.J.1    Mowbray, S.L.2
  • 17
    • 67849117365 scopus 로고    scopus 로고
    • Low-resolution structures of transient protein-protein complexes using small-angle X-ray scattering
    • J. Blobel, P. Bernado, D.I. Svergun, R. Tauler, and M. Pons Low-resolution structures of transient protein-protein complexes using small-angle X-ray scattering Journal of the American Chemical Society 131 2009 4378 4386
    • (2009) Journal of the American Chemical Society , vol.131 , pp. 4378-4386
    • Blobel, J.1    Bernado, P.2    Svergun, D.I.3    Tauler, R.4    Pons, M.5
  • 18
    • 34248567079 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase oligomerization studied by a combination of 15N NMR relaxation and 129Xe NMR. Effect of buffer containing arginine and glutamic acid
    • J. Blobel, S. Schmidl, D. Vidal, L. Nisius, P. Bernado, and O. Millet Protein tyrosine phosphatase oligomerization studied by a combination of 15N NMR relaxation and 129Xe NMR. Effect of buffer containing arginine and glutamic acid Journal of the American Chemical Society 129 2007 5946 5953
    • (2007) Journal of the American Chemical Society , vol.129 , pp. 5946-5953
    • Blobel, J.1    Schmidl, S.2    Vidal, D.3    Nisius, L.4    Bernado, P.5    Millet, O.6
  • 19
    • 33748781457 scopus 로고    scopus 로고
    • The dynamic energy landscape of dihydrofolate reductase catalysis
    • D.D. Boehr, D. McElheny, H.J. Dyson, and P.E. Wright The dynamic energy landscape of dihydrofolate reductase catalysis Science (New York, NY) 313 2006 1638 1642
    • (2006) Science (New York, NY) , vol.313 , pp. 1638-1642
    • Boehr, D.D.1    McElheny, D.2    Dyson, H.J.3    Wright, P.E.4
  • 21
    • 77956636052 scopus 로고    scopus 로고
    • The maltose ATP-binding cassette transporter in the 21st century - Towards a structural dynamic perspective on its mode of action
    • E. Bordignon, M. Grote, and E. Schneider The maltose ATP-binding cassette transporter in the 21st century - Towards a structural dynamic perspective on its mode of action Molecular Microbiology 77 2010 1354 1366
    • (2010) Molecular Microbiology , vol.77 , pp. 1354-1366
    • Bordignon, E.1    Grote, M.2    Schneider, E.3
  • 22
    • 34249781722 scopus 로고    scopus 로고
    • Conformational changes of glucose/galactose-binding protein illuminated by open, unliganded, and ultra-high-resolution ligand-bound structures
    • M.J. Borrok, L.L. Kiessling, and K.T. Forest Conformational changes of glucose/galactose-binding protein illuminated by open, unliganded, and ultra-high-resolution ligand-bound structures Protein Science 16 2007 1032 1041
    • (2007) Protein Science , vol.16 , pp. 1032-1041
    • Borrok, M.J.1    Kiessling, L.L.2    Forest, K.T.3
  • 24
    • 0029029566 scopus 로고
    • Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling
    • R. Bruschweiler, X. Liao, and P.E. Wright Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling Science (New York, NY) 268 1995 886 889
    • (1995) Science (New York, NY) , vol.268 , pp. 886-889
    • Bruschweiler, R.1    Liao, X.2    Wright, P.E.3
  • 25
    • 0028929925 scopus 로고
    • Large amplitude twisting motions of an interdomain hinge: A disulfide trapping study of the galactose-glucose binding protein
    • C.L. Careaga, J. Sutherland, J. Sabeti, and J.J. Falke Large amplitude twisting motions of an interdomain hinge: A disulfide trapping study of the galactose-glucose binding protein Biochemistry 34 1995 3048 3055
    • (1995) Biochemistry , vol.34 , pp. 3048-3055
    • Careaga, C.L.1    Sutherland, J.2    Sabeti, J.3    Falke, J.J.4
  • 26
    • 0021832329 scopus 로고
    • A major phosphotyrosyl-protein phosphatase from bovine heart is associated with a low-molecular-weight acid phosphatase
    • J. Chernoff, and H.C. Li A major phosphotyrosyl-protein phosphatase from bovine heart is associated with a low-molecular-weight acid phosphatase Archives of Biochemistry and Biophysics 240 1985 135 145
    • (1985) Archives of Biochemistry and Biophysics , vol.240 , pp. 135-145
    • Chernoff, J.1    Li, H.C.2
  • 27
    • 0025046144 scopus 로고
    • Deviations from the simple 2-parameter model-free approach to the interpretation of n-15 nuclear magnetic-relaxation of proteins
    • G.M. Clore, A. Szabo, A. Bax, L.E. Kay, P.C. Driscoll, and A.M. Gronenborn Deviations from the simple 2-parameter model-free approach to the interpretation of n-15 nuclear magnetic-relaxation of proteins Journal of the American Chemical Society 112 1990 4989 4991
    • (1990) Journal of the 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
  • 28
    • 38349077155 scopus 로고    scopus 로고
    • Optimisation of NMR dynamic models I. Minimisation algorithms and their performance within the model-free and Brownian rotational diffusion spaces
    • E.J. d'Auvergne, and P.R. Gooley Optimisation of NMR dynamic models I. Minimisation algorithms and their performance within the model-free and Brownian rotational diffusion spaces Journal of Biomolecular NMR 40 2008 107 119
    • (2008) Journal of Biomolecular NMR , vol.40 , pp. 107-119
    • D'Auvergne, E.J.1    Gooley, P.R.2
  • 29
    • 38349050193 scopus 로고    scopus 로고
    • Optimisation of NMR dynamic models II. A new methodology for the dual optimisation of the model-free parameters and the Brownian rotational diffusion tensor
    • E.J. d'Auvergne, and P.R. Gooley Optimisation of NMR dynamic models II. A new methodology for the dual optimisation of the model-free parameters and the Brownian rotational diffusion tensor Journal of Biomolecular NMR 40 2008 121 133
    • (2008) Journal of Biomolecular NMR , vol.40 , pp. 121-133
    • D'Auvergne, E.J.1    Gooley, P.R.2
  • 30
    • 77951298407 scopus 로고    scopus 로고
    • Models of macromolecular crowding effects and the need for quantitative comparisons with experiment
    • A.H. Elcock Models of macromolecular crowding effects and the need for quantitative comparisons with experiment Current Opinion in Structural Biology 20 2010 196 206
    • (2010) Current Opinion in Structural Biology , vol.20 , pp. 196-206
    • Elcock, A.H.1
  • 31
    • 0029102089 scopus 로고
    • Dynamics of the dihydrofolate reductase-folate complex: Catalytic sites and regions known to undergo conformational change exhibit diverse dynamical features
    • D.M. Epstein, S.J. Benkovic, and P.E. Wright Dynamics of the dihydrofolate reductase-folate complex: Catalytic sites and regions known to undergo conformational change exhibit diverse dynamical features Biochemistry 34 1995 11037 11048
    • (1995) Biochemistry , vol.34 , pp. 11037-11048
    • Epstein, D.M.1    Benkovic, S.J.2    Wright, P.E.3
  • 32
    • 3342925849 scopus 로고    scopus 로고
    • Methods to study protein dynamics and folding by mass spectrometry
    • S.J. Eyles, and I.A. Kaltashov Methods to study protein dynamics and folding by mass spectrometry Methods 34 2004 88 99
    • (2004) Methods , vol.34 , pp. 88-99
    • Eyles, S.J.1    Kaltashov, I.A.2
  • 34
    • 22144474407 scopus 로고    scopus 로고
    • On the origin of the thermostabilization of proteins induced by sodium phosphate
    • R. Fayos, M. Pons, and O. Millet On the origin of the thermostabilization of proteins induced by sodium phosphate Journal of the American Chemical Society 127 2005 9690 9691
    • (2005) Journal of the American Chemical Society , vol.127 , pp. 9690-9691
    • Fayos, R.1    Pons, M.2    Millet, O.3
  • 35
    • 0023668190 scopus 로고
    • Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli
    • C.A. Fierke, K.A. Johnson, and S.J. Benkovic Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli Biochemistry 26 1987 4085 4092
    • (1987) Biochemistry , vol.26 , pp. 4085-4092
    • Fierke, C.A.1    Johnson, K.A.2    Benkovic, S.J.3
  • 37
    • 0031566963 scopus 로고    scopus 로고
    • The main-chain dynamics of the dynamin pleckstrin homology (PH) domain in solution: Analysis of 15N relaxation with monomer/dimer equilibration
    • D. Fushman, S. Cahill, and D. Cowburn The main-chain dynamics of the dynamin pleckstrin homology (PH) domain in solution: Analysis of 15N relaxation with monomer/dimer equilibration Journal of Molecular Biology 266 1997 173 194
    • (1997) Journal of Molecular Biology , vol.266 , pp. 173-194
    • Fushman, D.1    Cahill, S.2    Cowburn, D.3
  • 39
    • 0034328380 scopus 로고    scopus 로고
    • HYDRONMR: Prediction of NMR relaxation of globular proteins from atomic-level structures and hydrodynamic calculations
    • J. Garcia de la Torre, M.L. Huertas, and B. Carrasco HYDRONMR: Prediction of NMR relaxation of globular proteins from atomic-level structures and hydrodynamic calculations Journal of Magnetic Resonance 147 2000 138 146
    • (2000) Journal of Magnetic Resonance , vol.147 , pp. 138-146
    • Garcia De La Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 40
    • 0031595590 scopus 로고    scopus 로고
    • The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins
    • K.H. Gardner, and L.E. Kay The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins Annual Review of Biophysics and Biomolecular Structure 27 1998 357 406
    • (1998) Annual Review of Biophysics and Biomolecular Structure , vol.27 , pp. 357-406
    • Gardner, K.H.1    Kay, L.E.2
  • 41
    • 0028335096 scopus 로고
    • Structural mechanisms for domain movements in proteins
    • M. Gerstein, A.M. Lesk, and C. Chothia Structural mechanisms for domain movements in proteins Biochemistry 33 1994 6739 6749
    • (1994) Biochemistry , vol.33 , pp. 6739-6749
    • Gerstein, M.1    Lesk, A.M.2    Chothia, C.3
  • 42
    • 24744470578 scopus 로고    scopus 로고
    • Probing the binding entropy of ligand-protein interactions by NMR
    • S.W. Homans Probing the binding entropy of ligand-protein interactions by NMR ChemBioChem 6 2005 1585 1591
    • (2005) ChemBioChem , vol.6 , pp. 1585-1591
    • Homans, S.W.1
  • 43
    • 6344231261 scopus 로고    scopus 로고
    • Rapid analysis of large protein-protein complexes using NMR-derived orientational constraints: The 95 kDa complex of LpxA with acyl carrier protein
    • N.U. Jain, T.J. Wyckoff, C.R. Raetz, and J.H. Prestegard Rapid analysis of large protein-protein complexes using NMR-derived orientational constraints: The 95 kDa complex of LpxA with acyl carrier protein Journal of Molecular Biology 343 2004 1379 1389
    • (2004) Journal of Molecular Biology , vol.343 , pp. 1379-1389
    • Jain, N.U.1    Wyckoff, T.J.2    Raetz, C.R.3    Prestegard, J.H.4
  • 45
    • 0037343308 scopus 로고    scopus 로고
    • Molecular dynamics of biological macromolecules: A brief history and perspective
    • M. Karplus Molecular dynamics of biological macromolecules: A brief history and perspective Biopolymers 68 2003 350 358
    • (2003) Biopolymers , vol.68 , pp. 350-358
    • Karplus, M.1
  • 46
    • 0024449503 scopus 로고
    • Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease
    • L.E. Kay, D.A. Torchia, and A. Bax Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease Biochemistry 28 1989 8972 8979
    • (1989) Biochemistry , vol.28 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 47
    • 79958837339 scopus 로고    scopus 로고
    • An introduction to NMR-based approaches for measuring protein dynamics
    • I.R. Kleckner, and M.P. Foster An introduction to NMR-based approaches for measuring protein dynamics Biochimica et Biophysica Acta 1814 2011 942 968
    • (2011) Biochimica et Biophysica Acta , vol.1814 , pp. 942-968
    • Kleckner, I.R.1    Foster, M.P.2
  • 48
    • 0345169163 scopus 로고    scopus 로고
    • Small-angle scattering: A view on the properties, structures and structural changes of biological macromolecules in solution
    • M.H. Koch, P. Vachette, and D.I. Svergun Small-angle scattering: A view on the properties, structures and structural changes of biological macromolecules in solution Quarterly Reviews of Biophysics 36 2003 147 227
    • (2003) Quarterly Reviews of Biophysics , vol.36 , pp. 147-227
    • Koch, M.H.1    Vachette, P.2    Svergun, D.I.3
  • 49
    • 42449102160 scopus 로고    scopus 로고
    • Probing invisible, low-populated States of protein molecules by relaxation dispersion NMR spectroscopy: An application to protein folding
    • D.M. Korzhnev, and L.E. Kay Probing invisible, low-populated States of protein molecules by relaxation dispersion NMR spectroscopy: An application to protein folding Accounts of Chemical Research 41 2008 442 451
    • (2008) Accounts of Chemical Research , vol.41 , pp. 442-451
    • Korzhnev, D.M.1    Kay, L.E.2
  • 50
    • 27644432794 scopus 로고    scopus 로고
    • Multiple-site exchange in proteins studied with a suite of six NMR relaxation dispersion experiments: An application to the folding of a Fyn SH3 domain mutant
    • D.M. Korzhnev, P. Neudecker, A. Mittermaier, V.Y. Orekhov, and L.E. Kay Multiple-site exchange in proteins studied with a suite of six NMR relaxation dispersion experiments: An application to the folding of a Fyn SH3 domain mutant Journal of the American Chemical Society 127 2005 15602 15611
    • (2005) Journal of the American Chemical Society , vol.127 , pp. 15602-15611
    • Korzhnev, D.M.1    Neudecker, P.2    Mittermaier, A.3    Orekhov, V.Y.4    Kay, L.E.5
  • 52
    • 10744221921 scopus 로고    scopus 로고
    • Temperature-dependent spectral density analysis applied to monitoring backbone dynamics of major urinary protein-I complexed with the pheromone 2-sec-butyl-4,5-dihydrothiazole
    • H. Krizova, L. Zidek, M.J. Stone, M.V. Novotny, and V. Sklenar Temperature-dependent spectral density analysis applied to monitoring backbone dynamics of major urinary protein-I complexed with the pheromone 2-sec-butyl-4,5-dihydrothiazole Journal of Biomolecular NMR 28 2004 369 384
    • (2004) Journal of Biomolecular NMR , vol.28 , pp. 369-384
    • Krizova, H.1    Zidek, L.2    Stone, M.J.3    Novotny, M.V.4    Sklenar, V.5
  • 53
    • 0031111153 scopus 로고    scopus 로고
    • Rotational diffusion anisotropy of proteins from simultaneous analysis of 15N and 13C alpha nuclear spin relaxation
    • L.K. Lee, M. Rance, W.J. Chazin, and A.G. Palmer 3rd. Rotational diffusion anisotropy of proteins from simultaneous analysis of 15N and 13C alpha nuclear spin relaxation Journal of Biomolecular NMR 9 1997 287 298
    • (1997) Journal of Biomolecular NMR , vol.9 , pp. 287-298
    • Lee, L.K.1    Rance, M.2    Chazin, W.J.3    Palmer III, A.G.4
  • 54
    • 77956361185 scopus 로고    scopus 로고
    • Three-dimensional structure of the weakly associated protein homodimer SeR13 using RDCs and paramagnetic surface mapping
    • H.W. Lee, G. Wylie, S. Bansal, X. Wang, A.W. Barb, and M.A. Macnaughtan Three-dimensional structure of the weakly associated protein homodimer SeR13 using RDCs and paramagnetic surface mapping Protein Science 19 2010 1673 1685
    • (2010) Protein Science , vol.19 , pp. 1673-1685
    • Lee, H.W.1    Wylie, G.2    Bansal, S.3    Wang, X.4    Barb, A.W.5    Macnaughtan, M.A.6
  • 55
    • 0029872895 scopus 로고    scopus 로고
    • Internal mobility in the partially folded DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral density functions
    • J.F. Lefevre, K.T. Dayie, J.W. Peng, and G. Wagner Internal mobility in the partially folded DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral density functions Biochemistry 35 1996 2674 2686
    • (1996) Biochemistry , vol.35 , pp. 2674-2686
    • Lefevre, J.F.1    Dayie, K.T.2    Peng, J.W.3    Wagner, G.4
  • 56
    • 33745842893 scopus 로고    scopus 로고
    • The solution structure of Escherichia coli Wzb reveals a novel substrate recognition mechanism of prokaryotic low molecular weight protein-tyrosine phosphatases
    • E. Lescop, Y. Hu, H. Xu, W. Hu, J. Chen, and B. Xia The solution structure of Escherichia coli Wzb reveals a novel substrate recognition mechanism of prokaryotic low molecular weight protein-tyrosine phosphatases The Journal of Biological Chemistry 281 2006 19570 19577
    • (2006) The Journal of Biological Chemistry , vol.281 , pp. 19570-19577
    • Lescop, E.1    Hu, Y.2    Xu, H.3    Hu, W.4    Chen, J.5    Xia, B.6
  • 57
    • 33646719091 scopus 로고
    • Model free approach to the interpretation of nuclear magnetic relaxation in macromolecules: 1. Theory and range of validity
    • G. Lipari, and A. Szabo Model free approach to the interpretation of nuclear magnetic relaxation in macromolecules: 1. Theory and range of validity Journal of the American Chemical Society 104 1982 4546 4559
    • (1982) Journal of the American Chemical Society , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 58
    • 40549133186 scopus 로고    scopus 로고
    • Characterization of enzyme motions by solution NMR relaxation dispersion
    • J.P. Loria, R.B. Berlow, and E.D. Watt Characterization of enzyme motions by solution NMR relaxation dispersion Accounts of Chemical Research 41 2008 214 221
    • (2008) Accounts of Chemical Research , vol.41 , pp. 214-221
    • Loria, J.P.1    Berlow, R.B.2    Watt, E.D.3
  • 59
    • 0033577288 scopus 로고    scopus 로고
    • A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy
    • J.P. Loria, M. Rance, and A.G. Palmer A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy Journal of the American Chemical Society 122 1999 2331 2332
    • (1999) Journal of the American Chemical Society , vol.122 , pp. 2331-2332
    • Loria, J.P.1    Rance, M.2    Palmer, A.G.3
  • 60
    • 0025821340 scopus 로고
    • Open conformation of a substrate-binding cleft: 19 F NMR studies of cleft angle in the D-galactose chemosensory receptor
    • L.A. Luck, and J.J. Falke Open conformation of a substrate-binding cleft: 19 F NMR studies of cleft angle in the D-galactose chemosensory receptor Biochemistry 30 1991 6484 6490
    • (1991) Biochemistry , vol.30 , pp. 6484-6490
    • Luck, L.A.1    Falke, J.J.2
  • 61
    • 34047136004 scopus 로고    scopus 로고
    • Global changes in local protein dynamics reduce the entropic cost of carbohydrate binding in the arabinose-binding protein
    • C.A. MacRaild, A.H. Daranas, A. Bronowska, and S.W. Homans Global changes in local protein dynamics reduce the entropic cost of carbohydrate binding in the arabinose-binding protein Journal of Molecular Biology 368 2007 822 832
    • (2007) Journal of Molecular Biology , vol.368 , pp. 822-832
    • Macraild, C.A.1    Daranas, A.H.2    Bronowska, A.3    Homans, S.W.4
  • 65
    • 0037051893 scopus 로고    scopus 로고
    • NMR measurement of the off rate from the first calcium-binding site of the synaptotagmin i C2A domain
    • O. Millet, P. Bernado, J. Garcia, J. Rizo, and M. Pons NMR measurement of the off rate from the first calcium-binding site of the synaptotagmin I C2A domain FEBS Letters 516 2002 93 96
    • (2002) FEBS Letters , vol.516 , pp. 93-96
    • Millet, O.1    Bernado, P.2    Garcia, J.3    Rizo, J.4    Pons, M.5
  • 67
    • 0034728579 scopus 로고    scopus 로고
    • The static magnetic field dependence of chemical exchange line broadening defines the NMR chemical shift time scale
    • O. Millet, J.P. Loria, C.D. Kroenke, M. Pons, and A.G. Palmer The static magnetic field dependence of chemical exchange line broadening defines the NMR chemical shift time scale Journal of the American Chemical Society 122 2000 2867 2877
    • (2000) Journal of the American Chemical Society , vol.122 , pp. 2867-2877
    • Millet, O.1    Loria, J.P.2    Kroenke, C.D.3    Pons, M.4    Palmer, A.G.5
  • 68
    • 0019883893 scopus 로고
    • Effect of macromolecular crowding upon the structure and function of an enzyme: Glyceraldehyde-3-phosphate dehydrogenase
    • A.P. Minton, and J. Wilf Effect of macromolecular crowding upon the structure and function of an enzyme: Glyceraldehyde-3-phosphate dehydrogenase Biochemistry 20 1981 4821 4826
    • (1981) Biochemistry , vol.20 , pp. 4821-4826
    • Minton, A.P.1    Wilf, J.2
  • 69
    • 33645834303 scopus 로고    scopus 로고
    • New tools provide new insights in NMR studies of protein dynamics
    • A. Mittermaier, and L.E. Kay New tools provide new insights in NMR studies of protein dynamics Science (New York, NY) 312 2006 224 228
    • (2006) Science (New York, NY) , vol.312 , pp. 224-228
    • Mittermaier, A.1    Kay, L.E.2
  • 70
    • 0035354587 scopus 로고    scopus 로고
    • Time-resolved biochemical crystallography: A mechanistic perspective
    • K. Moffat Time-resolved biochemical crystallography: A mechanistic perspective Chemical Reviews 101 2001 1569 1581
    • (2001) Chemical Reviews , vol.101 , pp. 1569-1581
    • Moffat, K.1
  • 71
    • 33746260426 scopus 로고    scopus 로고
    • Monitoring and modeling of protein processes using mass spectrometry, circular dichroism, and multivariate curve resolution methods
    • S. Navea, R. Tauler, and A. de Juan Monitoring and modeling of protein processes using mass spectrometry, circular dichroism, and multivariate curve resolution methods Analytical Chemistry 78 2006 4768 4778
    • (2006) Analytical Chemistry , vol.78 , pp. 4768-4778
    • Navea, S.1    Tauler, R.2    De Juan, A.3
  • 72
    • 66149129565 scopus 로고    scopus 로고
    • Relaxation dispersion NMR spectroscopy as a tool for detailed studies of protein folding
    • P. Neudecker, P. Lundstrom, and L.E. Kay Relaxation dispersion NMR spectroscopy as a tool for detailed studies of protein folding Biophysical Journal 96 2009 2045 2054
    • (2009) Biophysical Journal , vol.96 , pp. 2045-2054
    • Neudecker, P.1    Lundstrom, P.2    Kay, L.E.3
  • 73
    • 0000720448 scopus 로고
    • Backbone dynamics of (1-71)- and (1-36)bacterioopsin studied by two-dimensional (1)H- (15)N NMR spectroscopy
    • V.Y. Orekhov, K.V. Pervushin, D.M. Korzhnev, and A.S. Arseniev Backbone dynamics of (1-71)- and (1-36)bacterioopsin studied by two-dimensional (1)H- (15)N NMR spectroscopy Journal of Biomolecular NMR 6 1995 113 122
    • (1995) Journal of Biomolecular NMR , vol.6 , pp. 113-122
    • Orekhov, V.Y.1    Pervushin, K.V.2    Korzhnev, D.M.3    Arseniev, A.S.4
  • 75
    • 66249142325 scopus 로고    scopus 로고
    • Accurate characterization of weak macromolecular interactions by titration of NMR residual dipolar couplings: Application to the CD2AP SH3-C:ubiquitin complex
    • J.L. Ortega-Roldan, M.R. Jensen, B. Brutscher, A.I. Azuaga, M. Blackledge, and N.A. van Nuland Accurate characterization of weak macromolecular interactions by titration of NMR residual dipolar couplings: Application to the CD2AP SH3-C:ubiquitin complex Nucleic Acids Research 37 2009 e70
    • (2009) Nucleic Acids Research , vol.37 , pp. 70
    • Ortega-Roldan, J.L.1    Jensen, M.R.2    Brutscher, B.3    Azuaga, A.I.4    Blackledge, M.5    Van Nuland, N.A.6
  • 76
    • 0141746385 scopus 로고    scopus 로고
    • Diagnostic chemical shift markers for loop conformation and substrate and cofactor binding in dihydrofolate reductase complexes
    • M.J. Osborne, R.P. Venkitakrishnan, H.J. Dyson, and P.E. Wright Diagnostic chemical shift markers for loop conformation and substrate and cofactor binding in dihydrofolate reductase complexes Protein Science 12 2003 2230 2238
    • (2003) Protein Science , vol.12 , pp. 2230-2238
    • Osborne, M.J.1    Venkitakrishnan, R.P.2    Dyson, H.J.3    Wright, P.E.4
  • 77
    • 0034984208 scopus 로고    scopus 로고
    • Nmr probes of molecular dynamics: Overview and comparison with other techniques
    • A.G. Palmer 3rd. Nmr probes of molecular dynamics: Overview and comparison with other techniques Annual Review of Biophysics and Biomolecular Structure 30 2001 129 155
    • (2001) Annual Review of Biophysics and Biomolecular Structure , vol.30 , pp. 129-155
    • Palmer III, A.G.1
  • 78
    • 0029623152 scopus 로고
    • Frequency spectrum of NH bonds in eglin c from spectral density mapping at multiple fields
    • J.W. Peng, and G. Wagner Frequency spectrum of NH bonds in eglin c from spectral density mapping at multiple fields Biochemistry 34 1995 16733 16752
    • (1995) Biochemistry , vol.34 , pp. 16733-16752
    • Peng, J.W.1    Wagner, G.2
  • 80
    • 0029981539 scopus 로고    scopus 로고
    • Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: Variation of common themes
    • F.A. Quiocho, and P.S. Ledvina Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: Variation of common themes Molecular Microbiology 20 1996 17 25
    • (1996) Molecular Microbiology , vol.20 , pp. 17-25
    • Quiocho, F.A.1    Ledvina, P.S.2
  • 81
    • 0017914462 scopus 로고
    • Proton nuclear magnetic resonance in aqueous solutions
    • A.G. Redfield Proton nuclear magnetic resonance in aqueous solutions Methods in Enzymology 49 1978 253 270
    • (1978) Methods in Enzymology , vol.49 , pp. 253-270
    • Redfield, A.G.1
  • 83
    • 0031015737 scopus 로고    scopus 로고
    • Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence
    • M.R. Sawaya, and J. Kraut Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence Biochemistry 36 1997 586 603
    • (1997) Biochemistry , vol.36 , pp. 586-603
    • Sawaya, M.R.1    Kraut, J.2
  • 84
    • 0028541223 scopus 로고
    • A test of the model-free formulas. Effects of anisotropic rotational diffusion and dimerization
    • J.M. Schurr, H.P. Babcock, and B.S. Fujimoto A test of the model-free formulas. Effects of anisotropic rotational diffusion and dimerization Journal of Magnetic Resonance 105 1994 211 224
    • (1994) Journal of Magnetic Resonance , vol.105 , pp. 211-224
    • Schurr, J.M.1    Babcock, H.P.2    Fujimoto, B.S.3
  • 86
    • 0030606240 scopus 로고    scopus 로고
    • Conformational changes of three periplasmic receptors for bacterial chemotaxis and transport: The maltose-, glucose/galactose- and ribose-binding proteins
    • B.H. Shilton, M.M. Flocco, M. Nilsson, and S.L. Mowbray Conformational changes of three periplasmic receptors for bacterial chemotaxis and transport: The maltose-, glucose/galactose- and ribose-binding proteins Journal of Molecular Biology 264 1996 350 363
    • (1996) Journal of Molecular Biology , vol.264 , pp. 350-363
    • Shilton, B.H.1    Flocco, M.M.2    Nilsson, M.3    Mowbray, S.L.4
  • 88
    • 0037120879 scopus 로고    scopus 로고
    • Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments
    • N.R. Skrynnikov, F.W. Dahlquist, and L.E. Kay Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments Journal of the American Chemical Society 124 2002 12352 12360
    • (2002) Journal of the American Chemical Society , vol.124 , pp. 12352-12360
    • Skrynnikov, N.R.1    Dahlquist, F.W.2    Kay, L.E.3
  • 89
    • 0037024197 scopus 로고    scopus 로고
    • Deuterium spin probes of side-chain dynamics in proteins. 2. Spectral density mapping and identification of nanosecond time-scale side-chain motions
    • N.R. Skrynnikov, O. Millet, and L.E. Kay Deuterium spin probes of side-chain dynamics in proteins. 2. Spectral density mapping and identification of nanosecond time-scale side-chain motions Journal of the American Chemical Society 124 2002 6449 6460
    • (2002) Journal of the American Chemical Society , vol.124 , pp. 6449-6460
    • Skrynnikov, N.R.1    Millet, O.2    Kay, L.E.3
  • 91
    • 34548304719 scopus 로고    scopus 로고
    • Solution NMR of supramolecular complexes: Providing new insights into function
    • R. Sprangers, A. Velyvis, and L.E. Kay Solution NMR of supramolecular complexes: Providing new insights into function Nature Methods 4 2007 697 703
    • (2007) Nature Methods , vol.4 , pp. 697-703
    • Sprangers, R.1    Velyvis, A.2    Kay, L.E.3
  • 92
    • 0033533462 scopus 로고    scopus 로고
    • The structure of the bovine protein tyrosine phosphatase dimer reveals a potential self-regulation mechanism
    • L. Tabernero, B.N. Evans, P.A. Tishmack, R.L. Van Etten, and C.V. Stauffacher The structure of the bovine protein tyrosine phosphatase dimer reveals a potential self-regulation mechanism Biochemistry 38 1999 11651 11658
    • (1999) Biochemistry , vol.38 , pp. 11651-11658
    • Tabernero, L.1    Evans, B.N.2    Tishmack, P.A.3    Van Etten, R.L.4    Stauffacher, C.V.5
  • 93
    • 72249118262 scopus 로고    scopus 로고
    • Protein stabilization and the Hofmeister effect: The role of hydrophobic solvation
    • X. Tadeo, B. Lopez-Mendez, D. Castano, T. Trigueros, and O. Millet Protein stabilization and the Hofmeister effect: The role of hydrophobic solvation Biophysical Journal 97 2009 2595 2603
    • (2009) Biophysical Journal , vol.97 , pp. 2595-2603
    • Tadeo, X.1    Lopez-Mendez, B.2    Castano, D.3    Trigueros, T.4    Millet, O.5
  • 94
    • 41149167049 scopus 로고    scopus 로고
    • Visualization of transient ultra-weak protein self-association in solution using paramagnetic relaxation enhancement
    • C. Tang, R. Ghirlando, and G.M. Clore Visualization of transient ultra-weak protein self-association in solution using paramagnetic relaxation enhancement Journal of the American Chemical Society 130 2008 4048 4056
    • (2008) Journal of the American Chemical Society , vol.130 , pp. 4048-4056
    • Tang, C.1    Ghirlando, R.2    Clore, G.M.3
  • 95
    • 65249102824 scopus 로고    scopus 로고
    • Close encounters of the third kind: Disordered domains and the interactions of proteins
    • P. Tompa, M. Fuxreiter, C.J. Oldfield, I. Simon, A.K. Dunker, and V.N. Uversky Close encounters of the third kind: Disordered domains and the interactions of proteins Bioessays 31 2009 328 335
    • (2009) Bioessays , vol.31 , pp. 328-335
    • Tompa, P.1    Fuxreiter, M.2    Oldfield, C.J.3    Simon, I.4    Dunker, A.K.5    Uversky, V.N.6
  • 97
  • 100
    • 0023256886 scopus 로고
    • A novel calcium binding site in the galactose-binding protein of bacterial transport and chemotaxis
    • N.K. Vyas, M.N. Vyas, and F.A. Quiocho A novel calcium binding site in the galactose-binding protein of bacterial transport and chemotaxis Nature 327 1987 635 638
    • (1987) Nature , vol.327 , pp. 635-638
    • Vyas, N.K.1    Vyas, M.N.2    Quiocho, F.A.3
  • 101
    • 0024237631 scopus 로고
    • Sugar and signal-transducer binding sites of the Escherichia coli galactose chemoreceptor protein
    • N.K. Vyas, M.N. Vyas, and F.A. Quiocho Sugar and signal-transducer binding sites of the Escherichia coli galactose chemoreceptor protein Science (New York, NY) 242 1988 1290 1295
    • (1988) Science (New York, NY) , vol.242 , pp. 1290-1295
    • Vyas, N.K.1    Vyas, M.N.2    Quiocho, F.A.3
  • 102
    • 0025794052 scopus 로고
    • Comparison of the periplasmic receptors for L-arabinose, D-glucose/D-galactose, and D-ribose. Structural and Functional Similarity
    • N.K. Vyas, M.N. Vyas, and F.A. Quiocho Comparison of the periplasmic receptors for L-arabinose, D-glucose/D-galactose, and D-ribose. Structural and Functional Similarity The Journal of Biological Chemistry 266 1991 5226 5237
    • (1991) The Journal of Biological Chemistry , vol.266 , pp. 5226-5237
    • Vyas, N.K.1    Vyas, M.N.2    Quiocho, F.A.3
  • 103
    • 0023908621 scopus 로고
    • Purification and physicochemical characterization of a human placental acid phosphatase possessing phosphotyrosyl protein phosphatase activity
    • A. Waheed, P.M. Laidler, Y.Y. Wo, and R.L. Van Etten Purification and physicochemical characterization of a human placental acid phosphatase possessing phosphotyrosyl protein phosphatase activity Biochemistry 27 1988 4265 4273
    • (1988) Biochemistry , vol.27 , pp. 4265-4273
    • Waheed, A.1    Laidler, P.M.2    Wo, Y.Y.3    Van Etten, R.L.4
  • 105
    • 0037126686 scopus 로고    scopus 로고
    • Proline cis-trans isomerization and protein folding
    • W.J. Wedemeyer, E. Welker, and H.A. Scheraga Proline cis-trans isomerization and protein folding Biochemistry 41 2002 14637 14644
    • (2002) Biochemistry , vol.41 , pp. 14637-14644
    • Wedemeyer, W.J.1    Welker, E.2    Scheraga, H.A.3
  • 106
    • 0032493859 scopus 로고    scopus 로고
    • Switching signals on or off by receptor dimerization
    • A. Weiss, and J. Schlessinger Switching signals on or off by receptor dimerization Cell 94 1998 277 280
    • (1998) Cell , vol.94 , pp. 277-280
    • Weiss, A.1    Schlessinger, J.2
  • 108
    • 32444448489 scopus 로고    scopus 로고
    • Solution structure of a low-molecular-weight protein tyrosine phosphatase from Bacillus subtilis
    • H. Xu, B. Xia, and C. Jin Solution structure of a low-molecular-weight protein tyrosine phosphatase from Bacillus subtilis Journal of Bacteriology 188 2006 1509 1517
    • (2006) Journal of Bacteriology , vol.188 , pp. 1509-1517
    • Xu, H.1    Xia, B.2    Jin, C.3
  • 109
    • 0035799320 scopus 로고    scopus 로고
    • 15N NMR relaxation studies of backbone dynamics in free and steroid-bound Delta 5-3-ketosteroid isomerase from Pseudomonas testosteroni
    • S. Yun, D.S. Jang, D.H. Kim, K.Y. Choi, and H.C. Lee 15N NMR relaxation studies of backbone dynamics in free and steroid-bound Delta 5-3-ketosteroid isomerase from Pseudomonas testosteroni Biochemistry 40 2001 3967 3973
    • (2001) Biochemistry , vol.40 , pp. 3967-3973
    • Yun, S.1    Jang, D.S.2    Kim, D.H.3    Choi, K.Y.4    Lee, H.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.