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Volumn 45, Issue 8, 2006, Pages 2636-2647

Enzyme dynamics along the reaction coordinate: Critical role of a conserved residue

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL REACTIONS; CONFORMATIONS; DATA ACQUISITION; ENZYMES; NUCLEAR MAGNETIC RESONANCE; SUBSTRATES;

EID: 33644556820     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0525066     Document Type: Article
Times cited : (68)

References (70)
  • 1
    • 0030601792 scopus 로고    scopus 로고
    • Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: Application to protein folding
    • Yang, D., and Kay, L. E. (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.E.2
  • 2
    • 0030473440 scopus 로고    scopus 로고
    • Insights into the local residual entropy of proteins provided by NMR relaxation
    • Li, Z., Raychaudhuri, S., and Wand, A. J. (1996) Insights into the local residual entropy of proteins provided by NMR relaxation, Protein Sci. 5, 2647-2650.
    • (1996) Protein Sci. , vol.5 , pp. 2647-2650
    • Li, Z.1    Raychaudhuri, S.2    Wand, A.J.3
  • 4
    • 0030299991 scopus 로고    scopus 로고
    • 15N NMR relaxation studies of free and inhibitor-bound 4-oxalocrotonate tautomerase: Backbone dynamics and entropy changes of an enzyme upon inhibitor binding
    • 15N NMR relaxation studies of free and inhibitor-bound 4-oxalocrotonate tautomerase: Backbone dynamics and entropy changes of an enzyme upon inhibitor binding, Biochemistry 35, 16036-16047.
    • (1996) Biochemistry , vol.35 , pp. 16036-16047
    • Stivers, J.T.1    Abeygunawardana, C.2    Mildvan, A.S.3
  • 5
    • 0032710610 scopus 로고    scopus 로고
    • Increased protein backbone conformational entropy upon hydrophobic ligand binding
    • Zidek, L., Novotny, M. V., and Stone, M. J. (1999) Increased protein backbone conformational entropy upon hydrophobic ligand binding, Nat. Struct. Biol. 6, 1118-1121.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 1118-1121
    • Zidek, L.1    Novotny, M.V.2    Stone, M.J.3
  • 6
    • 0038219675 scopus 로고    scopus 로고
    • Temperature dependence of the backbone dynamics of ribonuclease a in the ground state and bound to the inhibitor 5′-phosphothymidine (3′-5′) pyrophosphate adenosine 3′-phosphate
    • Kovrigin, E. L., Cole, R., and Loria, J. P. (2003) Temperature dependence of the backbone dynamics of ribonuclease A in the ground state and bound to the inhibitor 5′-phosphothymidine (3′-5′) pyrophosphate adenosine 3′-phosphate, Biochemistry 42, 5279-5291.
    • (2003) Biochemistry , vol.42 , pp. 5279-5291
    • Kovrigin, E.L.1    Cole, R.2    Loria, J.P.3
  • 7
    • 0033525126 scopus 로고    scopus 로고
    • Temperature dependence of intramolecular dynamics of the basic leucine zipper of GCN4: Implications for the entropy of association with DNA
    • Bracken, C., Carr, P. A., Cavanagh, J., and Palmer, A. G. (1999) Temperature dependence of intramolecular dynamics of the basic leucine zipper of GCN4: Implications for the entropy of association with DNA, J. Mol. Biol. 285, 2133-2146.
    • (1999) J. Mol. Biol. , vol.285 , pp. 2133-2146
    • Bracken, C.1    Carr, P.A.2    Cavanagh, J.3    Palmer, A.G.4
  • 8
    • 0033988897 scopus 로고    scopus 로고
    • Redistribution and loss of side chain entropy upon formation of a calmodulin-peptide complex
    • Lee, A. L., Kinnear, S. A., and Wand, A. J. (2000) Redistribution and loss of side chain entropy upon formation of a calmodulin-peptide complex, Nat. Struct. Biol. 7, 72-77.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 72-77
    • Lee, A.L.1    Kinnear, S.A.2    Wand, A.J.3
  • 9
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionarily conserved pathways of energetic connectivity in protein families
    • Lockless, S. W., and Ranganathan, R. (1999) Evolutionarily conserved pathways of energetic connectivity in protein families, Science 286, 295-299.
    • (1999) Science , vol.286 , pp. 295-299
    • Lockless, S.W.1    Ranganathan, R.2
  • 10
    • 0037219686 scopus 로고    scopus 로고
    • Evolutionarily conserved networks of residues mediate allosteric communication in proteins
    • Suel, G. M., Lockless, S. W., Wall, M. A., and Ranganathan, R. (2003) Evolutionarily conserved networks of residues mediate allosteric communication in proteins, Nat. Struct. Biol. 10, 59-69.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 59-69
    • Suel, G.M.1    Lockless, S.W.2    Wall, M.A.3    Ranganathan, R.4
  • 11
    • 0034760077 scopus 로고    scopus 로고
    • Dynamic activation of protein function: A view emerging from NMR spectrscopy
    • Wand, A. J. (2001) Dynamic activation of protein function: A view emerging from NMR spectrscopy, Nat. Struct. Biol. 8, 926-931.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 926-931
    • Wand, A.J.1
  • 12
    • 0347753736 scopus 로고    scopus 로고
    • Ligand-dependent dynamics and intramolecular signaling in a PDZ domain
    • Fuentes, E. J., Der, C. J., and Lee, A. L. (2004) Ligand-dependent dynamics and intramolecular signaling in a PDZ domain, J. Mol. Biol. 335, 1105-1115.
    • (2004) J. Mol. Biol. , vol.335 , pp. 1105-1115
    • Fuentes, E.J.1    Der, C.J.2    Lee, A.L.3
  • 14
    • 0035928796 scopus 로고    scopus 로고
    • Backbone dynamics in dihydrofolate reductase complexes: Role of loop flexibility in the catalytic mechanism
    • Osborne, M. J., Schnell, J., Benkovic, S. J., Dyson, H. J., and Wright, P. E. (2001) Backbone dynamics in dihydrofolate reductase complexes: Role of loop flexibility in the catalytic mechanism, Biochemistry 40, 9846-9859.
    • (2001) Biochemistry , vol.40 , pp. 9846-9859
    • Osborne, M.J.1    Schnell, J.2    Benkovic, S.J.3    Dyson, H.J.4    Wright, P.E.5
  • 15
    • 11144328151 scopus 로고    scopus 로고
    • Conformational changes in the active site loops of dihydrofolate reductase during the catalytic cycle
    • Venkitakrishnan, R. P., Zaborowski, E., McElheny, D., Benkovic, S. J., Dyson, H. J., and Wright, P. E. (2004) Conformational changes in the active site loops of dihydrofolate reductase during the catalytic cycle, Biochemistry 43, 16046-16055.
    • (2004) Biochemistry , vol.43 , pp. 16046-16055
    • Venkitakrishnan, R.P.1    Zaborowski, E.2    Mcelheny, D.3    Benkovic, S.J.4    Dyson, H.J.5    Wright, P.E.6
  • 16
    • 0037076522 scopus 로고    scopus 로고
    • Evidence for flexibility in the function of ribonuclease A
    • Cole, R., and 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
  • 17
    • 21244440196 scopus 로고    scopus 로고
    • Conservation of μs-ms enzyme motions in the apo- and substrate-mimicked state
    • Beach, H., Cole, R., Gill, M., and Loria, J. P. (2005) Conservation of μs-ms enzyme motions in the apo- and substrate-mimicked state, J. Am. Chem. Soc. 127, 9167-9176.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 9167-9176
    • Beach, H.1    Cole, R.2    Gill, M.3    Loria, J.P.4
  • 18
    • 0035078116 scopus 로고    scopus 로고
    • Dynamics of the transition between open and closed conformations in a calmodulin C-terminal domain mutant
    • Evenas, J., Malmendal, A., and Akke, M. (2001) Dynamics of the transition between open and closed conformations in a calmodulin C-terminal domain mutant, Structure 9, 185-195.
    • (2001) Structure , vol.9 , pp. 185-195
    • Evenas, J.1    Malmendal, A.2    Akke, M.3
  • 19
    • 0035819455 scopus 로고    scopus 로고
    • 15N relaxation dispersion NMR spectroscopy: Application to Asn and Gln residues in a cavity mutant of T4 lysozyme
    • 15N relaxation dispersion NMR spectroscopy: Application to Asn and Gln residues in a cavity mutant of T4 lysozyme, J. Am. Chem. Soc. 123, 967-975.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 967-975
    • Mulder, F.A.1    Skrynnikov, N.R.2    Hon, B.3    Dahlquist, F.W.4    Kay, L.E.5
  • 20
    • 0347997288 scopus 로고    scopus 로고
    • Local protein dynamics and catalysis: Detection of segmental motion associated with rate-limiting product release by a glutathione transferase
    • Codreanu, S. G., Ladner, J. E., Xiao, G. Y., Stourman, N. V., Hachey, D. L., Gilliland, G. L., and Armstrong, R. N. (2002) Local protein dynamics and catalysis: Detection of segmental motion associated with rate-limiting product release by a glutathione transferase, Biochemistry 41, 15161-15172.
    • (2002) Biochemistry , vol.41 , pp. 15161-15172
    • Codreanu, S.G.1    Ladner, J.E.2    Xiao, G.Y.3    Stourman, N.V.4    Hachey, D.L.5    Gilliland, G.L.6    Armstrong, R.N.7
  • 21
    • 0345306309 scopus 로고    scopus 로고
    • Disulfide bond isomerization in basic pancreatic trypsin inhibitor: Multisite chemical exchange quantified by CPMG relaxation dispersion and chemical shift modeling
    • Grey, M. J., Wang, C., and Palmer, A. G., III (2003) Disulfide bond isomerization in basic pancreatic trypsin inhibitor: Multisite chemical exchange quantified by CPMG relaxation dispersion and chemical shift modeling, J. Am. Chem. Soc. 125, 14324-14335.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 14324-14335
    • Grey, M.J.1    Wang, C.2    Palmer III, A.G.3
  • 24
    • 0034730994 scopus 로고    scopus 로고
    • Molecular motions and protein folding: Characterization of the backbone dynamics and folding equilibrium of α D-2 using C-13 NMR spin relaxation
    • Hill, R. B., Bracken, C., DeGrado, W. F., and Palmer, A. G. (2000) Molecular motions and protein folding: Characterization of the backbone dynamics and folding equilibrium of α D-2 using C-13 NMR spin relaxation, J. Am. Chem. Soc. 122, 11610-11619.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 11610-11619
    • Hill, R.B.1    Bracken, C.2    DeGrado, W.F.3    Palmer, A.G.4
  • 25
    • 0036416144 scopus 로고    scopus 로고
    • TROSY-NMR studies of the 91 kDa TRAP protein reveal allosteric control of a gene regulatory protein by ligand-altered flexibility
    • McElroy, C., Manfredo, A., Wendt, A., Gollnick, P., and Foster, M. (2002) TROSY-NMR studies of the 91 kDa TRAP protein reveal allosteric control of a gene regulatory protein by ligand-altered flexibility, J. Mol. Biol. 323, 463-473.
    • (2002) J. Mol. Biol. , vol.323 , pp. 463-473
    • Mcelroy, C.1    Manfredo, A.2    Wendt, A.3    Gollnick, P.4    Foster, M.5
  • 26
    • 0034765285 scopus 로고    scopus 로고
    • Delineation of the allosteric mechanism of a cytidylyltransferase exhibiting negative cooperativity
    • Stevens, S. Y., Sanker, S., Kent, C., and Zuiderweg, E. R. (2001) Delineation of the allosteric mechanism of a cytidylyltransferase exhibiting negative cooperativity, Nat. Struct. Biol. 8, 947-952.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 947-952
    • Stevens, S.Y.1    Sanker, S.2    Kent, C.3    Zuiderweg, E.R.4
  • 27
    • 0033566242 scopus 로고    scopus 로고
    • Millisecond-time-scale motions contribute to the function of the bacterial response regulator protein Spo0F
    • Feher, V. A., and Cavanagh, J. (1999) Millisecond-time-scale motions contribute to the function of the bacterial response regulator protein Spo0F, Nature 400, 289-293.
    • (1999) Nature , vol.400 , pp. 289-293
    • Feher, V.A.1    Cavanagh, J.2
  • 28
    • 0037457884 scopus 로고    scopus 로고
    • Identification of a PU.1-IRF4 protein interaction surface predicted by chemical exchange line broadening
    • McKercher, S. R., Lombardo, C. R., Bobkov, A., Jia, X., and AssaMunt, N. (2003) Identification of a PU.1-IRF4 protein interaction surface predicted by chemical exchange line broadening, Proc. Natl. Acad. Sci. U.S.A. 100, 511-516.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 511-516
    • Mckercher, S.R.1    Lombardo, C.R.2    Bobkov, A.3    Jia, X.4    AssaMunt, N.5
  • 29
    • 23044501324 scopus 로고    scopus 로고
    • PhosphoThr peptide binding globally rigidifies much of the FHA domain from arabidopsis receptor kinase-associated protein phosphatase
    • Ding, Z., Lee, G., Liang, X., Gallazzi, F., Arunima, A., and van Doren, S. R. (2005) PhosphoThr peptide binding globally rigidifies much of the FHA domain from arabidopsis receptor kinase-associated protein phosphatase, Biochemistry 44, 10119-10134.
    • (2005) Biochemistry , vol.44 , pp. 10119-10134
    • Ding, Z.1    Lee, G.2    Liang, X.3    Gallazzi, F.4    Arunima, A.5    Van Doren, S.R.6
  • 30
    • 0033544709 scopus 로고    scopus 로고
    • Changes in side-chain and backbone dynamics identify determinants of specificity in RNA recognition by human U1A protein
    • Mittermaier, A., Varani, L., Muhandiram, D. R., Kay, L. E., and Varani, G. (1999) Changes in side-chain and backbone dynamics identify determinants of specificity in RNA recognition by human U1A protein, J. Mol. Biol. 294, 967-979.
    • (1999) J. Mol. Biol. , vol.294 , pp. 967-979
    • Mittermaier, A.1    Varani, L.2    Muhandiram, D.R.3    Kay, L.E.4    Varani, G.5
  • 31
    • 0028985308 scopus 로고
    • Human type-α transforming growth factor undergoes slow conformational exchange between multiple backbone conformations as characterized by nitrogen-15 relaxation measurements
    • Li, Y.-C, and Montelione, G. T. (1995) Human type-α transforming growth factor undergoes slow conformational exchange between multiple backbone conformations as characterized by nitrogen-15 relaxation measurements, Biochemistry 34, 2408-2423.
    • (1995) Biochemistry , vol.34 , pp. 2408-2423
    • Li, Y.-C.1    Montelione, G.T.2
  • 32
    • 0038169722 scopus 로고
    • Relaxation spectra of ribonuclease. I. The interaction of ribonuclease with cytidine 3′-phosphate
    • Cathou, R. E., and Hammes, G. G. (1965) Relaxation spectra of ribonuclease. I. The interaction of ribonuclease with cytidine 3′-phosphate, J. Am. Chem. Soc. 86, 3240-3245.
    • (1965) J. Am. Chem. Soc. , vol.86 , pp. 3240-3245
    • Cathou, R.E.1    Hammes, G.G.2
  • 33
    • 0037008011 scopus 로고    scopus 로고
    • Multiple conformational changes in enzyme catalysis
    • Hammes, G. G. (2002) Multiple conformational changes in enzyme catalysis, Biochemistry 41, 8221-8228.
    • (2002) Biochemistry , vol.41 , pp. 8221-8228
    • Hammes, G.G.1
  • 34
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod, J., Wyman, J., and Changeux, J.-P. (1965) On the nature of allosteric transitions: A plausible model, J. Mol. Biol. 12, 88-118.
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.-P.3
  • 35
    • 33947445379 scopus 로고
    • A theory of the structure and process of formation of antibodies
    • Pauling, L. (1940) A theory of the structure and process of formation of antibodies, J. Am. Chem. Soc. 62, 2643-2657.
    • (1940) J. Am. Chem. Soc. , vol.62 , pp. 2643-2657
    • Pauling, L.1
  • 36
    • 0015223374 scopus 로고
    • Equilibrium and rate constants for the interconversion of two conformations of chymotrypsin. The existence of a catalytically inactive conformation at neutral pH
    • Fersht, A. R., and Requena, Y. (1971) Equilibrium and rate constants for the interconversion of two conformations of chymotrypsin. The existence of a catalytically inactive conformation at neutral pH, J. Mol. Biol. 60, 279-290.
    • (1971) J. Mol. Biol. , vol.60 , pp. 279-290
    • Fersht, A.R.1    Requena, Y.2
  • 38
    • 0029000872 scopus 로고
    • Dynamics of the flexible loop of triosephosphate isomerase: The loop motion is not ligand gated
    • Williams, J. C., and McDermott, A. E. (1995) Dynamics of the flexible loop of triosephosphate isomerase: The loop motion is not ligand gated, Biochemistry 34, 8309-8319.
    • (1995) Biochemistry , vol.34 , pp. 8309-8319
    • Williams, J.C.1    McDermott, A.E.2
  • 39
    • 0013843341 scopus 로고
    • Relaxation spectra of ribonuclease. III. Further investigation of the interaction of ribonuclease and cytidine 3′-phosphate
    • Cathou, R. E., and Hammes, G. G. (1965) Relaxation spectra of ribonuclease. III. Further investigation of the interaction of ribonuclease and cytidine 3′-phosphate, J. Am. Chem. Soc. 87, 4674-4680.
    • (1965) J. Am. Chem. Soc. , vol.87 , pp. 4674-4680
    • Cathou, R.E.1    Hammes, G.G.2
  • 40
    • 0026720247 scopus 로고
    • Crystalline ribonuclease a loses function below the dynamical transition at 220 K
    • Rasmussen, B. F., Stock, A. M., Ringe, D., and Petsko, G. A. (1992) Crystalline ribonuclease A loses function below the dynamical transition at 220 K, Nature 357, 423-424.
    • (1992) Nature , vol.357 , pp. 423-424
    • Rasmussen, B.F.1    Stock, A.M.2    Ringe, D.3    Petsko, G.A.4
  • 41
    • 0032560446 scopus 로고    scopus 로고
    • His-Asp catalytic dyad of ribonuclease A: Structure and function of the wild-type, D121N, and D121A enzymes
    • Schultz, L. W., Quirk, D. J., and Raines, R. T. (1998) His-Asp catalytic dyad of ribonuclease A: Structure and function of the wild-type, D121N, and D121A enzymes, Biochemistry 37, 8886-8898.
    • (1998) Biochemistry , vol.37 , pp. 8886-8898
    • Schultz, L.W.1    Quirk, D.J.2    Raines, R.T.3
  • 42
    • 0024291642 scopus 로고
    • Structure of phosphate-free ribonuclease A refined at 1.26 Å
    • Wlodawer, A., Svensson, L. A., Sjolin, L., and Gilliland, G. L. (1988) Structure of phosphate-free ribonuclease A refined at 1.26 Å, Biochemistry 27, 2705-2717.
    • (1988) Biochemistry , vol.27 , pp. 2705-2717
    • Wlodawer, A.1    Svensson, L.A.2    Sjolin, L.3    Gilliland, G.L.4
  • 44
    • 0022515682 scopus 로고
    • The mechanism of binding of a polynucleotide chain to pancreatic ribonuclease
    • McPherson, A., Brayer, G., Cascio, D., and Williams, R. (1986) The mechanism of binding of a polynucleotide chain to pancreatic ribonuclease, Science 232, 765-768.
    • (1986) Science , vol.232 , pp. 765-768
    • Mcpherson, A.1    Brayer, G.2    Cascio, D.3    Williams, R.4
  • 45
    • 0022452886 scopus 로고
    • Kinetic studies on turtle pancreatic ribonuclease-A comparative study of the base specificities of the B2 and P0 sites of bovine pancreatic ribonuclease-A and turtle pancreatic ribonuclease
    • Katoh, H., Yoshinaga, M., Yanagita, T., Ohgi, K., Irie, M., Beintema, J. J., and Meinsma, D. (1986) Kinetic studies on turtle pancreatic ribonuclease-A comparative study of the base specificities of the B2 and P0 sites of bovine pancreatic ribonuclease-A and turtle pancreatic ribonuclease, Biochim. Biophys. Acta 873, 367-371.
    • (1986) Biochim. Biophys. Acta , vol.873 , pp. 367-371
    • Katoh, H.1    Yoshinaga, M.2    Yanagita, T.3    Ohgi, K.4    Irie, M.5    Beintema, J.J.6    Meinsma, D.7
  • 47
    • 0028564999 scopus 로고
    • The structures of RNase a complexed with 3′-CMP and d(CpA): Active site conformation and conserved water molecules
    • Zegers, I., Maes, D., Dao-Thi, M. H., Poortmans, F., Palmer, R., and Wyns, L. (1994) The structures of RNase A complexed with 3′-CMP and d(CpA): Active site conformation and conserved water molecules, Protein Sci. 3, 2322-2339.
    • (1994) Protein Sci. , vol.3 , pp. 2322-2339
    • Zegers, I.1    Maes, D.2    Dao-Thi, M.H.3    Poortmans, F.4    Palmer, R.5    Wyns, L.6
  • 48
    • 0032589144 scopus 로고    scopus 로고
    • a values in the wild-type, D121N, and D121A enzymes
    • a values in the wild-type, D121N, and D121A enzymes, Biophys. J. 76, 1571-1579.
    • (1999) Biophys. J. , vol.76 , pp. 1571-1579
    • Quirk, D.J.1    Raines, R.T.2
  • 49
    • 0033543235 scopus 로고    scopus 로고
    • Toward rational design of ribonuclease inhibitors: High-resolution crystal structure of a ribonuclease A complex with a potent 3′,5′- pyrophosphate-linked dinucleotide inhibitor
    • Leonidas, D. D., Shapiro, R., Irons, L. I., Russo, N., and Acharya, K. R. (1999) Toward rational design of ribonuclease inhibitors: High-resolution crystal structure of a ribonuclease A complex with a potent 3′,5′- pyrophosphate-linked dinucleotide inhibitor, Biochemistry 38, 10287-10297.
    • (1999) Biochemistry , vol.38 , pp. 10287-10297
    • Leonidas, D.D.1    Shapiro, R.2    Irons, L.I.3    Russo, N.4    Acharya, K.R.5
  • 50
    • 0033577288 scopus 로고    scopus 로고
    • A Relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy
    • Loria, J. P., Rance, M., and Palmer, A. G. (1999) A Relaxation- compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy, J. Am. Chem. Soc. 121, 2331-2332.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 2331-2332
    • Loria, J.P.1    Rance, M.2    Palmer, A.G.3
  • 53
    • 0001766423 scopus 로고
    • 2 relaxation - The multisite case
    • 2 relaxation - The multisite case, J. Magn. Reson. 30, 111-128.
    • (1978) J. Magn. Reson. , vol.30 , pp. 111-128
    • Jen, J.1
  • 55
    • 0037120879 scopus 로고    scopus 로고
    • Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments
    • Skrynnikov, N. R., Dahlquist, F. W., and Kay, L. E. (2002) Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments, J. Am. Chem. Soc. 124, 12352-12360.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 12352-12360
    • Skrynnikov, N.R.1    Dahlquist, F.W.2    Kay, L.E.3
  • 57
    • 0345517099 scopus 로고    scopus 로고
    • 3J-coupling analysis for the joint calibration of Karplus coefficients and evaluation of torsion angles
    • 3J-coupling analysis for the joint calibration of Karplus coefficients and evaluation of torsion angles, J. Biomol. NMR 14, 1-12.
    • (1999) J. Biomol. NMR , vol.14 , pp. 1-12
    • Schmidt, J.M.1    Blumel, M.2    Lohr, F.3    Ruterjans, H.4
  • 61
    • 33645929731 scopus 로고    scopus 로고
    • Faithful estimation of dynamics parameters from relaxation dispersion measurements
    • in press
    • Kovrigin, E. L., Kempf, J. G., Grey, M., and Loria, J. P. (2005) Faithful estimation of dynamics parameters from relaxation dispersion measurements, J. Magn. Reson., in press.
    • (2005) J. Magn. Reson.
    • Kovrigin, E.L.1    Kempf, J.G.2    Grey, M.3    Loria, J.P.4
  • 63
    • 0038148710 scopus 로고    scopus 로고
    • Conformational diversity and protein evolution - A 60-year-old hypothesis revisited
    • James, L. C., and Tawfik, D. S. (2003) Conformational diversity and protein evolution - A 60-year-old hypothesis revisited, Trends Biochem. Sci. 28, 361-368.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 361-368
    • James, L.C.1    Tawfik, D.S.2
  • 65
    • 0031443372 scopus 로고    scopus 로고
    • Evidence for a functional role of the dynamics of glycine-121 of Escherichia coli dihydrofolate reductase obtained from kinetic analysis of a site-directed mutant
    • Cameron, C. E., and Benkovic, S. J. (1997) Evidence for a functional role of the dynamics of glycine-121 of Escherichia coli dihydrofolate reductase obtained from kinetic analysis of a site-directed mutant, Biochemistry 36, 15792-15800.
    • (1997) Biochemistry , vol.36 , pp. 15792-15800
    • Cameron, C.E.1    Benkovic, S.J.2
  • 66
  • 67
    • 0027511809 scopus 로고
    • High-resolution three-dimensional structure of ribonuclease A in solution by nuclear magnetic resonance spectroscopy
    • Santoro, J., Gonzalez, C., Bruix, M., Neira, J. L., Nieto, J. L., Herranz, J., and Rico, M. (1993) High-resolution three-dimensional structure of ribonuclease A in solution by nuclear magnetic resonance spectroscopy, J. Mol. Biol. 229, 722-734.
    • (1993) J. Mol. Biol. , vol.229 , pp. 722-734
    • Santoro, J.1    Gonzalez, C.2    Bruix, M.3    Neira, J.L.4    Nieto, J.L.5    Herranz, J.6    Rico, M.7
  • 68
    • 33845182844 scopus 로고
    • 2D chemical exchange NMR spectroscopy by proton-detected heteronuclear correlation
    • Montelione, G. T., and Wagner, G. (1989) 2D chemical exchange NMR spectroscopy by proton-detected heteronuclear correlation, J. Am. Chem. Soc. 111, 3096-3098.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 3096-3098
    • Montelione, G.T.1    Wagner, G.2
  • 69
    • 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., and Wuthrich, K. (1991) Studies of slow conformational equilibria in macromolecules by exchange of heteronuclear longitudinal 2-spin-order in a 2D difference correlation experiment, J. Biomol. NMR 1, 93-98.
    • (1991) J. Biomol. NMR , vol.1 , pp. 93-98
    • Wider, G.1    Neri, D.2    Wuthrich, K.3
  • 70
    • 0028503463 scopus 로고
    • 15N longitudinal decay and chemical exchange rates of systems in slow equilibrium
    • 15N longitudinal decay and chemical exchange rates of systems in slow equilibrium, J. Biomol. NMR 4, 727-734.
    • (1994) J. Biomol. NMR , vol.4 , pp. 727-734
    • Farrow, N.1    Zhang, O.2    Forman-Kay, J.D.3    Kay, L.E.4


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