메뉴 건너뛰기




Volumn 44, Issue 18, 2005, Pages 6788-6799

Investigation of ligand binding and protein dynamics in Bacillus subtilis chorismate mutase by transverse relaxation optimized spectroscopy-nuclear magnetic resonance

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CATALYSIS; CONFORMATIONS; DIFFUSION; MICROORGANISMS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

EID: 18244376600     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0474259     Document Type: Article
Times cited : (25)

References (80)
  • 1
    • 0025189923 scopus 로고
    • Monofunctional chorismate mutase from Bacillus subtilis: Purification of the protein, molecular cloning of the gene, and overexpression of the gene product in Escherichia coli
    • Gray, J. V., Golinellipimpaneau, B., and Knowles, J. R. (1990) Monofunctional chorismate mutase from Bacillus subtilis: Purification of the protein, molecular cloning of the gene, and overexpression of the gene product in Escherichia coli, Biochemistry 29, 376-383.
    • (1990) Biochemistry , vol.29 , pp. 376-383
    • Gray, J.V.1    Golinellipimpaneau, B.2    Knowles, J.R.3
  • 2
    • 0027335927 scopus 로고
    • C-13 NMR studies of the enzyme product complex of Bacillus subtilis chorismate mutase
    • Rajagopalan, J. S., Taylor, K. M., and Jaffe, E. K. (1993) C-13 NMR studies of the enzyme product complex of Bacillus subtilis chorismate mutase, Biochemistry 32, 3965-3972.
    • (1993) Biochemistry , vol.32 , pp. 3965-3972
    • Rajagopalan, J.S.1    Taylor, K.M.2    Jaffe, E.K.3
  • 3
    • 0028106685 scopus 로고
    • Monofunctional chorismate mutase from Bacillus subtilis: FTIR studies and the mechanism of action of the enzyme
    • Gray, J. V., and Knowles, J. R. (1994) Monofunctional chorismate mutase from Bacillus subtilis: FTIR studies and the mechanism of action of the enzyme, Biochemistry 33, 9953-9959.
    • (1994) Biochemistry , vol.33 , pp. 9953-9959
    • Gray, J.V.1    Knowles, J.R.2
  • 4
    • 0029927729 scopus 로고    scopus 로고
    • Mutagenesis study of active site residues in chorismate mutase from Bacillus subtilis
    • Cload, S. T., Liu, D. R., Pastor, R. M., and Schultz, P. G. (1996) Mutagenesis study of active site residues in chorismate mutase from Bacillus subtilis, J. Am. Chem. Soc. 118, 1787-1788.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 1787-1788
    • Cload, S.T.1    Liu, D.R.2    Pastor, R.M.3    Schultz, P.G.4
  • 5
    • 0030058137 scopus 로고    scopus 로고
    • Electrostatic catalysis of the Claisen rearrangement: Probing the role of Glu78 in Bacillus subtilis chorismate mutase by genetic selection
    • Kast, P., Hartgerink, J. D., AsifUllah, M., and Hilvert, D. (1996) Electrostatic catalysis of the Claisen rearrangement: Probing the role of Glu78 in Bacillus subtilis chorismate mutase by genetic selection, J. Am. Chem. Soc. 118, 3069-3070.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 3069-3070
    • Kast, P.1    Hartgerink, J.D.2    Asifullah, M.3    Hilvert, D.4
  • 6
    • 0029928213 scopus 로고    scopus 로고
    • Is chorismate mutase a prototypic entropy trap? Activation parameters for the Bacillus subtilis enzyme
    • Kast, P., AsifUllah, M., and Hilvert, D. (1996) Is chorismate mutase a prototypic entropy trap? Activation parameters for the Bacillus subtilis enzyme, Tetrahedron Lett. 37, 2691-2694.
    • (1996) Tetrahedron Lett. , vol.37 , pp. 2691-2694
    • Kast, P.1    AsifUllah, M.2    Hilvert, D.3
  • 7
    • 0031360609 scopus 로고    scopus 로고
    • Thermodynamics of the conversion of chorismate to prephenate: Experimental results and theoretical predictions
    • Kast, P., Tewari, Y. B., Wiest, O., Hilvert, D., Houk, K. N., and Goldberg, R. N. (1997) Thermodynamics of the conversion of chorismate to prephenate: Experimental results and theoretical predictions, J. Phys. Chem. B 101, 10976-10982.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 10976-10982
    • Kast, P.1    Tewari, Y.B.2    Wiest, O.3    Hilvert, D.4    Houk, K.N.5    Goldberg, R.N.6
  • 8
    • 0033118836 scopus 로고    scopus 로고
    • Bacillus subtilis chorismate mutase is partially diffusion-controlled
    • Mattei, P., Kast, P., and Hilvert, D. (1999) Bacillus subtilis chorismate mutase is partially diffusion-controlled, Eur. J. Biochem. 261, 25-32.
    • (1999) Eur. J. Biochem. , vol.261 , pp. 25-32
    • Mattei, P.1    Kast, P.2    Hilvert, D.3
  • 9
    • 0034711227 scopus 로고    scopus 로고
    • A strategically positioned cation is crucial for efficient catalysis by chorismate mutase
    • Kast, P., Grisostomi, C., Chen, I. A., Li, S. L., Krengel, U., Xue, Y. F., and Hilvert, D. (2000) A strategically positioned cation is crucial for efficient catalysis by chorismate mutase, J. Biol. Chem. 275, 36832-36838.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36832-36838
    • Kast, P.1    Grisostomi, C.2    Chen, I.A.3    Li, S.L.4    Krengel, U.5    Xue, Y.F.6    Hilvert, D.7
  • 10
    • 0142052240 scopus 로고    scopus 로고
    • Selective stabilization of the chorismate mutase transition state by a positively charged hydrogen bond donor
    • Kienhöfer, A., Kast, P., and Hilvert, D. (2003) Selective stabilization of the chorismate mutase transition state by a positively charged hydrogen bond donor, J. Am. Chem. Soc. 125, 3206-3207.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 3206-3207
    • Kienhöfer, A.1    Kast, P.2    Hilvert, D.3
  • 11
    • 0037621429 scopus 로고    scopus 로고
    • Charge optimization increases the potency and selectivity of a chorismate mutase inhibitor
    • Mandal, A., and Hilvert, D. (2003) Charge optimization increases the potency and selectivity of a chorismate mutase inhibitor, J. Am. Chem. Soc. 125, 5598-5599.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 5598-5599
    • Mandal, A.1    Hilvert, D.2
  • 12
    • 0027274818 scopus 로고
    • Crystal structures of the monofunctional chorismate mutase from Bacillus subtilis and its complex with a transition-state analog
    • Chook, Y. M., Ke, H. M., and Lipscomb, W. N. (1993) Crystal structures of the monofunctional chorismate mutase from Bacillus subtilis and its complex with a transition-state analog, Proc. Natl. Acad. Sci. U.S.A. 90, 8600-8603.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 8600-8603
    • Chook, Y.M.1    Ke, H.M.2    Lipscomb, W.N.3
  • 13
    • 0027992458 scopus 로고
    • The monofunctional chorismate mutase from Bacillus subtilis: Structure determination of chorismate mutase and its complexes with a transition-state analog and prephenate, and implications for the mechanism of the enzymatic reaction
    • Chook, Y. M., Gray, J. V., Ke, H. M., and Lipscomb, W. N. (1994) The monofunctional chorismate mutase from Bacillus subtilis: Structure determination of chorismate mutase and its complexes with a transition-state analog and prephenate, and implications for the mechanism of the enzymatic reaction, J. Mol. Biol. 240, 476-500.
    • (1994) J. Mol. Biol. , vol.240 , pp. 476-500
    • Chook, Y.M.1    Gray, J.V.2    Ke, H.M.3    Lipscomb, W.N.4
  • 14
    • 0034096989 scopus 로고    scopus 로고
    • The 1.30 Å resolution structure of the Bacillus subtilis chorismate mutase catalytic homotrimer
    • Ladner, J. E., Reddy, P., Davis, A., Tordova, M., Howard, A. J., and Gilliland, G. L. (2000) The 1.30 Å resolution structure of the Bacillus subtilis chorismate mutase catalytic homotrimer, Acta Crystallogr. D56, 673-683.
    • (2000) Acta Crystallogr. , vol.D56 , pp. 673-683
    • Ladner, J.E.1    Reddy, P.2    Davis, A.3    Tordova, M.4    Howard, A.J.5    Gilliland, G.L.6
  • 15
    • 0029174681 scopus 로고
    • Stabilization of the transition state of the chorismate prephenate rearrangement: An ab initio study of enzyme and antibody catalysis
    • Wiest, O., and Houk, K. N. (1995) Stabilization of the transition state of the chorismate prephenate rearrangement: An ab initio study of enzyme and antibody catalysis, J. Am. Chem. Soc. 117, 11628-11639.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 11628-11639
    • Wiest, O.1    Houk, K.N.2
  • 16
    • 0037419004 scopus 로고    scopus 로고
    • Understanding the role of active-site residues in chorismate mutase catalysis from molecular-dynamics simulations
    • Guo, H., Cui, Q., Lipscomb, W. N., and Karplus, M. (2003) Understanding the role of active-site residues in chorismate mutase catalysis from molecular-dynamics simulations, Angew. Chem., Int. Ed. 42, 1508-1511.
    • (2003) Angew. Chem., Int. Ed. , vol.42 , pp. 1508-1511
    • Guo, H.1    Cui, Q.2    Lipscomb, W.N.3    Karplus, M.4
  • 17
    • 0035979270 scopus 로고    scopus 로고
    • Substrate conformational transitions in the active site of chorismate mutase: Their role in the catalytic mechanism
    • Guo, H., Cui, Q., Lipscomb, W. N., and Karplus, M. (2001) Substrate conformational transitions in the active site of chorismate mutase: Their role in the catalytic mechanism, Proc. Natl. Acad. Sci. U.S.A. 98, 9032-9037.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 9032-9037
    • Guo, H.1    Cui, Q.2    Lipscomb, W.N.3    Karplus, M.4
  • 18
    • 0037450070 scopus 로고    scopus 로고
    • Preorganization and reorganization as related factors in enzyme catalysis: The chorismate mutase case
    • Marti, S., Andres, J., Moliner, V., Silla, E., Tunon, I., and Bertran, J. (2003) Preorganization and reorganization as related factors in enzyme catalysis: The chorismate mutase case, Chem.-Eur. J. 9, 984-991.
    • (2003) Chem.-Eur. J. , vol.9 , pp. 984-991
    • Marti, S.1    Andres, J.2    Moliner, V.3    Silla, E.4    Tunon, I.5    Bertran, J.6
  • 19
    • 0347129735 scopus 로고    scopus 로고
    • A comparative study of Claisen and Cope rearrangements catalyzed by chorismate mutase. An insight into enzymatic efficiency: Transition state stabilization or substrate preorganization?
    • Marti, S., Andres, J., Moliner, V., Silla, E., Tunon, I., and Bertran, J. (2004) A comparative study of Claisen and Cope rearrangements catalyzed by chorismate mutase. An insight into enzymatic efficiency: Transition state stabilization or substrate preorganization? J. Am. Chem. Soc. 126, 311-319.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 311-319
    • Marti, S.1    Andres, J.2    Moliner, V.3    Silla, E.4    Tunon, I.5    Bertran, J.6
  • 20
    • 0042355696 scopus 로고    scopus 로고
    • Just a near attack conformer for catalysis (chorismate to prephenate rearrangements in water, antibody, enzymes, and their mutants)
    • Hur, S., and Bruice, T. C. (2003) Just a near attack conformer for catalysis (chorismate to prephenate rearrangements in water, antibody, enzymes, and their mutants), J. Am. Chem. Soc. 125, 10540-10542.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 10540-10542
    • Hur, S.1    Bruice, T.C.2
  • 21
    • 0142091405 scopus 로고    scopus 로고
    • The near attack conformation approach to the study of the chorismate to prephenate reaction
    • Hur, S., and Bruice, T. C. (2003) The near attack conformation approach to the study of the chorismate to prephenate reaction, Proc. Natl. Acad. Sci. U.S.A. 100, 12015-12020.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 12015-12020
    • Hur, S.1    Bruice, T.C.2
  • 22
    • 0037153275 scopus 로고    scopus 로고
    • Reaction mechanism of chorismate mutase studied by the combined potentials of quantum mechanics and molecular mechanics
    • Lee, Y. S., Worthington, S. E., Krauss, M., and Brooks, B. R. (2002) Reaction mechanism of chorismate mutase studied by the combined potentials of quantum mechanics and molecular mechanics, J. Phys. Chem. B 106, 12059-12065.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 12059-12065
    • Lee, Y.S.1    Worthington, S.E.2    Krauss, M.3    Brooks, B.R.4
  • 23
    • 0000167881 scopus 로고
    • Insights into chorismate mutase catalysis from a combined QM/MM simulation of the enzyme reaction
    • Lyne, P. D., Mulholland, A. J., and Richards, W. G. (1995) Insights into chorismate mutase catalysis from a combined QM/MM simulation of the enzyme reaction, J. Am. Chem. Soc. 117, 11345-11350.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 11345-11350
    • Lyne, P.D.1    Mulholland, A.J.2    Richards, W.G.3
  • 24
    • 2942739060 scopus 로고    scopus 로고
    • Conformational effects in enzyme catalysis: QM/MM free energy calculation of the 'NAC' contribution in chorismate mutase
    • Ranaghan, K. E., and Mulholland, A. J. (2004) Conformational effects in enzyme catalysis: QM/MM free energy calculation of the 'NAC' contribution in chorismate mutase, Chem. Commun., 1238-1239.
    • (2004) Chem. Commun. , pp. 1238-1239
    • Ranaghan, K.E.1    Mulholland, A.J.2
  • 25
    • 2342565009 scopus 로고    scopus 로고
    • Transition state stabilization and substrate strain in enzyme catalysis: Ab initio QM/MM modelling of the chorismate mutase reaction
    • Ranaghan, K. E., Ridder, L., Szefczyk, B., Sokalski, W. A., Hermann, J. C., and Mulholland, A. J. (2004) Transition state stabilization and substrate strain in enzyme catalysis: Ab initio QM/MM modelling of the chorismate mutase reaction, Org. Biomol. Chem. 2, 968-980.
    • (2004) Org. Biomol. Chem. , vol.2 , pp. 968-980
    • Ranaghan, K.E.1    Ridder, L.2    Szefczyk, B.3    Sokalski, W.A.4    Hermann, J.C.5    Mulholland, A.J.6
  • 26
    • 10344265555 scopus 로고    scopus 로고
    • Differential transition-state stabilization in enzyme catalysis: Quantum chemical analysis of interactions in the chorismate mutase reaction and prediction of the optimal catalytic field
    • Szefczyk, B., Mulholland, A. J., Ranaghan, K. E., and Sokalski, W. A. (2004) Differential transition-state stabilization in enzyme catalysis: Quantum chemical analysis of interactions in the chorismate mutase reaction and prediction of the optimal catalytic field, J. Am. Chem. Soc. 126, 16148-16159.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 16148-16159
    • Szefczyk, B.1    Mulholland, A.J.2    Ranaghan, K.E.3    Sokalski, W.A.4
  • 27
    • 0001664117 scopus 로고    scopus 로고
    • Aspects of hybrid QM/MM calculations: The treatment of the QM/MM interface region and geometry optimization with an application to chorismate mutase
    • Hall, R. J., Hindle, S. A., Burton, N. A., and Hillier, I. H. (2000) Aspects of hybrid QM/MM calculations: The treatment of the QM/MM interface region and geometry optimization with an application to chorismate mutase, J. Comput. Chem. 21, 1433-1441.
    • (2000) J. Comput. Chem. , vol.21 , pp. 1433-1441
    • Hall, R.J.1    Hindle, S.A.2    Burton, N.A.3    Hillier, I.H.4
  • 28
    • 0034824313 scopus 로고    scopus 로고
    • Electrostatic complementarity at ligand binding sites: Application to chorismate mutase
    • Kangas, E., and Tidor, B. (2001) Electrostatic complementarity at ligand binding sites: Application to chorismate mutase, J. Phys. Chem. B 105, 880-888.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 880-888
    • Kangas, E.1    Tidor, B.2
  • 29
    • 0346885688 scopus 로고    scopus 로고
    • A DFT-based QM-MM approach designed for the treatment of large molecular systems: Application to chorismate mutase
    • Crespo, A., Scherlis, D. A., Marti, M. A., Ordejon, P., Roitberg, A. E., and Estrin, D. A. (2003) A DFT-based QM-MM approach designed for the treatment of large molecular systems: Application to chorismate mutase, J. Phys. Chem. B 107, 13728-13736.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 13728-13736
    • Crespo, A.1    Scherlis, D.A.2    Marti, M.A.3    Ordejon, P.4    Roitberg, A.E.5    Estrin, D.A.6
  • 30
    • 0038615889 scopus 로고    scopus 로고
    • Contributions of conformational compression and preferential transition state stabilization to the rate enhancement by chorismate mutase
    • Guimaraes, C. R. W., Repasky, M. P., Chandrasekhar, J., Tirado-Rives, J., and Jorgensen, W. L. (2003) Contributions of conformational compression and preferential transition state stabilization to the rate enhancement by chorismate mutase, J. Am. Chem. Soc. 125, 6892-6899.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6892-6899
    • Guimaraes, C.R.W.1    Repasky, M.P.2    Chandrasekhar, J.3    Tirado-Rives, J.4    Jorgensen, W.L.5
  • 31
    • 0041429611 scopus 로고    scopus 로고
    • Apparent NAC effect in chorismate mutase reflects electrostatic transition state stabilization
    • Strajbl, M., Shurki, A., Kato, M., and Warshel, A. (2003) Apparent NAC effect in chorismate mutase reflects electrostatic transition state stabilization, J. Am. Chem. Soc. 125, 10228-10237.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 10228-10237
    • Strajbl, M.1    Shurki, A.2    Kato, M.3    Warshel, A.4
  • 32
    • 33845280929 scopus 로고
    • Chorismate mutase inhibitors: Synthesis and evaluation of some potential transition-state analogs
    • Bartlett, P. A., Nakagawa, Y., Johnson, C. R., Reich, S. H., and Luis, A. (1988) Chorismate mutase inhibitors: Synthesis and evaluation of some potential transition-state analogs, J. Org. Chem. 53, 3195-3210.
    • (1988) J. Org. Chem. , vol.53 , pp. 3195-3210
    • Bartlett, P.A.1    Nakagawa, Y.2    Johnson, C.R.3    Reich, S.H.4    Luis, A.5
  • 33
    • 0034700263 scopus 로고    scopus 로고
    • Probing the role of the C-terminus of Bacillus subtilis chorismate mutase by a novel random protein-termination strategy
    • Gamper, M., Hilvert, D., and Kast, P. (2000) Probing the role of the C-terminus of Bacillus subtilis chorismate mutase by a novel random protein-termination strategy, Biochemistry 39, 14087-14094.
    • (2000) Biochemistry , vol.39 , pp. 14087-14094
    • Gamper, M.1    Hilvert, D.2    Kast, P.3
  • 36
    • 0033167995 scopus 로고    scopus 로고
    • Exploring the dynamic information content of a protein NMR structure: Comparison of a molecular dynamics simulation with the NMR and X-ray structures of Escherichia coli ribonuclease HI
    • Philippopoulos, M., and Lim, C. (1999) Exploring the dynamic information content of a protein NMR structure: Comparison of a molecular dynamics simulation with the NMR and X-ray structures of Escherichia coli ribonuclease HI, Proteins 36, 87-110.
    • (1999) Proteins , vol.36 , pp. 87-110
    • Philippopoulos, M.1    Lim, C.2
  • 37
    • 0030612833 scopus 로고    scopus 로고
    • 2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • 2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution, Proc. Natl. Acad. Sci. U.S.A. 94, 12366-12371.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wüthrich, K.4
  • 38
    • 0033757115 scopus 로고    scopus 로고
    • Sequence-specific NMR assignment of proteins by global, fragment mapping with the program MAPPER
    • Guntert, P., Salzmann, M., Braun, D., and Wüthrich, K. (2000) Sequence-specific NMR assignment of proteins by global, fragment mapping with the program MAPPER, J. Biomol. NMR 18, 129-137.
    • (2000) J. Biomol. NMR , vol.18 , pp. 129-137
    • Guntert, P.1    Salzmann, M.2    Braun, D.3    Wüthrich, K.4
  • 39
    • 0032544978 scopus 로고    scopus 로고
    • Solution NMR studies of a 42 KDa Escherichia coli maltose binding protein β-cyclodextrin complex: Chemical shift assignments and analysis
    • Gardner, K. H., Zhang, X. C., Gehring, K., and Kay, L. E. (1998) Solution NMR studies of a 42 KDa Escherichia coli maltose binding protein β-cyclodextrin complex: Chemical shift assignments and analysis, J. Am. Chem. Soc. 120, 11738-11748.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 11738-11748
    • Gardner, K.H.1    Zhang, X.C.2    Gehring, K.3    Kay, L.E.4
  • 40
    • 0034625918 scopus 로고    scopus 로고
    • NMR assignment and secondary structure determination of an octameric 110 kDa protein using TROSY in triple resonance experiments
    • Salzmann, M., Pervushin, K., Wider, G., Senn, H., and Wüthrich, K. (2000) NMR assignment and secondary structure determination of an octameric 110 kDa protein using TROSY in triple resonance experiments, J. Am. Chem. Soc. 122, 7543-7548.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 7543-7548
    • Salzmann, M.1    Pervushin, K.2    Wider, G.3    Senn, H.4    Wüthrich, K.5
  • 41
    • 0034927940 scopus 로고    scopus 로고
    • TROSY NMR with partially deuterated proteins
    • Eletsky, A., Kienhöfer, A., and Pervushin, K. (2001) TROSY NMR with partially deuterated proteins, J. Biomol. NMR 20, 177-180.
    • (2001) J. Biomol. NMR , vol.20 , pp. 177-180
    • Eletsky, A.1    Kienhöfer, A.2    Pervushin, K.3
  • 42
    • 0037325758 scopus 로고    scopus 로고
    • A new strategy for backbone resonance assignment in large proteins using a MQ-HACACO experiment
    • Pervushin, K., and Eletsky, A. (2003) A new strategy for backbone resonance assignment in large proteins using a MQ-HACACO experiment, J. Biomol. NMR 25, 147-152.
    • (2003) J. Biomol. NMR , vol.25 , pp. 147-152
    • Pervushin, K.1    Eletsky, A.2
  • 43
    • 0038026909 scopus 로고    scopus 로고
    • Backbone resonance assignment in large protonated proteins using a combination of new 3D TROSY-HN(CA)HA, 4D TROSY-HACANH and C-13-detected HACACO experiments
    • Hu, K. F., Eletsky, A., and Pervushin, K. (2003) Backbone resonance assignment in large protonated proteins using a combination of new 3D TROSY-HN(CA)HA, 4D TROSY-HACANH and C-13-detected HACACO experiments, J. Biomol. NMR 26, 69-77.
    • (2003) J. Biomol. NMR , vol.26 , pp. 69-77
    • Hu, K.F.1    Eletsky, A.2    Pervushin, K.3
  • 44
    • 0036756444 scopus 로고    scopus 로고
    • Direct NMR observation and DFT calculations of a hydrogen bond at the active site of a 44 kDa enzyme
    • Eletsky, A., Heinz, T., Moreira, O., Kienhöfer, A., Hilvert, D., and Pervushin, K. (2002) Direct NMR observation and DFT calculations of a hydrogen bond at the active site of a 44 kDa enzyme, J. Biomol. NMR 24, 31-39.
    • (2002) J. Biomol. NMR , vol.24 , pp. 31-39
    • Eletsky, A.1    Heinz, T.2    Moreira, O.3    Kienhöfer, A.4    Hilvert, D.5    Pervushin, K.6
  • 45
    • 0038324522 scopus 로고    scopus 로고
    • A novel strategy for the assignment of side-chain resonances in completely deuterated large proteins using C-13 spectroscopy
    • Eletsky, A., Moreira, O., Kovacs, H., and Pervushin, K. (2003) A novel strategy for the assignment of side-chain resonances in completely deuterated large proteins using C-13 spectroscopy, J. Biomol. NMR 26, 167-179.
    • (2003) J. Biomol. NMR , vol.26 , pp. 167-179
    • Eletsky, A.1    Moreira, O.2    Kovacs, H.3    Pervushin, K.4
  • 46
    • 0037192915 scopus 로고    scopus 로고
    • Semi-classical nuclear spin relaxation theory revisited for use with biological macromolecules
    • Luginbuhl, P., and Wüthrich, K. (2002) Semi-classical nuclear spin relaxation theory revisited for use with biological macromolecules, Prog. Nucl. Magn. Reson. Spectrosc. 40, 199-247.
    • (2002) Prog. Nucl. Magn. Reson. Spectrosc. , vol.40 , pp. 199-247
    • Luginbuhl, P.1    Wüthrich, K.2
  • 48
    • 0141502348 scopus 로고    scopus 로고
    • Characterization of the overall and local dynamics of a protein with intermediate rotational anisotropy: Differentiating between conformational exchange and anisotropic diffusion in the B3 domain of protein G
    • Hall, J. B., and Fushman, D. (2003) Characterization of the overall and local dynamics of a protein with intermediate rotational anisotropy: Differentiating between conformational exchange and anisotropic diffusion in the B3 domain of protein G, J. Biomol. NMR 27, 261-275.
    • (2003) J. Biomol. NMR , vol.27 , pp. 261-275
    • Hall, J.B.1    Fushman, D.2
  • 50
    • 0024402002 scopus 로고
    • Model-independent and model-dependent analysis of the global and internal dynamics of cyclosporine-A
    • Dellwo, M. J., and Wand, A. J. (1989) Model-independent and model-dependent analysis of the global and internal dynamics of cyclosporine-A, J. Am. Chem. Soc. 111, 4571-4578.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 4571-4578
    • Dellwo, M.J.1    Wand, A.J.2
  • 52
    • 0026711032 scopus 로고
    • Fast internal main-chain dynamics of human ubiquitin
    • Schneider, D. M., Dellwo, M. J., and Wand, A. J. (1992) Fast internal main-chain dynamics of human ubiquitin, Biochemistry 31, 3645-3652.
    • (1992) Biochemistry , vol.31 , pp. 3645-3652
    • Schneider, D.M.1    Dellwo, M.J.2    Wand, A.J.3
  • 54
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia coli ribonuclease-H1: Correlations with structure and function in an active enzyme
    • Mandel, A. M., Akke, M., and Palmer, A. G. (1995) Backbone dynamics of Escherichia coli ribonuclease-H1: Correlations with structure and function in an active enzyme, J. Cell. Biochem., 29.
    • (1995) J. Cell. Biochem. , pp. 29
    • Mandel, A.M.1    Akke, M.2    Palmer, A.G.3
  • 55
    • 0037266991 scopus 로고    scopus 로고
    • The use of model selection in the model-free analysis of protein dynamics
    • d'Auvergne, E. J., and Gooley, P. R. (2003) The use of model selection in the model-free analysis of protein dynamics, J. Biomol. NMR 25, 25-39.
    • (2003) J. Biomol. NMR , vol.25 , pp. 25-39
    • D'Auvergne, E.J.1    Gooley, P.R.2
  • 57
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wüthrich, K. (1996) MOLMOL: A program for display and analysis of macromolecular structures, J. Mol. Graphics 14, 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 59
    • 0030217514 scopus 로고    scopus 로고
    • Nuclear magnetic resonance studies of biopolymer dynamics
    • Palmer, A. G., Williams, J., and McDermott, A. (1996) Nuclear magnetic resonance studies of biopolymer dynamics, J. Phys. Chem. 100, 13293-13310.
    • (1996) J. Phys. Chem. , vol.100 , pp. 13293-13310
    • Palmer, A.G.1    Williams, J.2    McDermott, A.3
  • 60
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules. 1. Theory and range of validity
    • Lipari, G., and Szabo, A. (1982) 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
  • 61
    • 33845553743 scopus 로고
    • Model-Free Approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules. 2. Analysis of experimental results
    • Lipari, G., and Szabo, A. (1982) Model-Free Approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules. 2. Analysis of experimental results, J. Am. Chem. Soc. 104, 4559-4570.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4559-4570
    • Lipari, G.1    Szabo, A.2
  • 64
    • 0037176836 scopus 로고    scopus 로고
    • 13C) NMR relaxation and computational molecular dynamics
    • 13C) NMR relaxation and computational molecular dynamics, Biochemistry 41, 2655-2666.
    • (2002) Biochemistry , vol.41 , pp. 2655-2666
    • Pang, Y.1    Buck, M.2    Zuiderweg, E.R.P.3
  • 67
    • 0031585744 scopus 로고    scopus 로고
    • Experimental characterization of models for backbone picosecond dynamics in proteins. Quantification of NMR auto- and cross-correlation relaxation mechanisms involving different nuclei of the peptide plane
    • Fischer, M. W. F., Zeng, L., Pang, Y. X., Hu, W. D., Majumdar, A., and Zuiderweg, E. R. P. (1997) Experimental characterization of models for backbone picosecond dynamics in proteins. Quantification of NMR auto- and cross-correlation relaxation mechanisms involving different nuclei of the peptide plane, J. Am. Chem. Soc. 119, 12629-12642.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 12629-12642
    • Fischer, M.W.F.1    Zeng, L.2    Pang, Y.X.3    Hu, W.D.4    Majumdar, A.5    Zuiderweg, E.R.P.6
  • 68
    • 0038037171 scopus 로고    scopus 로고
    • Temperature dependence of anisotropic protein backbone dynamics
    • Wang, T. Z., Cai, S., and Zuiderweg, E. R. P. (2003) Temperature dependence of anisotropic protein backbone dynamics, J. Am. Chem. Soc. 125, 8639-8643.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 8639-8643
    • Wang, T.Z.1    Cai, S.2    Zuiderweg, E.R.P.3
  • 69
    • 0029999832 scopus 로고    scopus 로고
    • Exploring the active site of chorismate mutase by combinatorial mutagenesis and selection: The importance of electrostatic catalysis
    • Kast, P., AsifUllah, M., Jiang, N., and Hilvert, D. (1996) Exploring the active site of chorismate mutase by combinatorial mutagenesis and selection: The importance of electrostatic catalysis, Proc. Natl. Acad. Sci. U.S.A. 93, 5043-5048.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 5043-5048
    • Kast, P.1    Asifullah, M.2    Jiang, N.3    Hilvert, D.4
  • 70
    • 0032516484 scopus 로고    scopus 로고
    • A small, thermostable, and monofunctional chorismate mutase from the archeon Methanococcus jannaschii
    • MacBeath, G., Kast, P., and Hilvert, D. (1998) A small, thermostable, and monofunctional chorismate mutase from the archeon Methanococcus jannaschii, Biochemistry 37, 10062-10073.
    • (1998) Biochemistry , vol.37 , pp. 10062-10073
    • MacBeath, G.1    Kast, P.2    Hilvert, D.3
  • 71
    • 0000088628 scopus 로고
    • Processing of multidimensional NMR data with the new software prosa
    • Guntert, P., Dötsch, V., Wider, G., and Wüthrich, K. (1992) Processing of multidimensional NMR data with the new software prosa, J. Biomol. NMR 2, 619-629.
    • (1992) J. Biomol. NMR , vol.2 , pp. 619-629
    • Guntert, P.1    Dötsch, V.2    Wider, G.3    Wüthrich, K.4
  • 72
    • 0343459675 scopus 로고
    • The program Xeasy for computer-supported NMR spectral-analysis of biological macromolecules
    • Bartels, C., Xia, T. H., Billeter, M., Guntert, P., and Wüthrich, K. (1995) The program Xeasy for computer-supported NMR spectral-analysis of biological macromolecules, J. Biomol. NMR 6, 1-10.
    • (1995) J. Biomol. NMR , vol.6 , pp. 1-10
    • Bartels, C.1    Xia, T.H.2    Billeter, M.3    Guntert, P.4    Wüthrich, K.5
  • 74
    • 0033518575 scopus 로고    scopus 로고
    • TROSY-type triple-resonance experiments for sequential NMR assignments of large proteins
    • Salzmann, M., Wider, G., Pervushin, K., Senn, H., and Wüthrich, K. (1999) TROSY-type triple-resonance experiments for sequential NMR assignments of large proteins, J. Am. Chem. Soc. 121, 844-848.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 844-848
    • Salzmann, M.1    Wider, G.2    Pervushin, K.3    Senn, H.4    Wüthrich, K.5
  • 75
    • 0000517056 scopus 로고
    • Improved linear prediction for truncated signals of known phase
    • Zhu, G., and Bax, A. (1990) Improved linear prediction for truncated signals of known phase, J. Magn. Reson. 90, 405-410.
    • (1990) J. Magn. Reson. , vol.90 , pp. 405-410
    • Zhu, G.1    Bax, A.2
  • 77
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia coli ribonuclease HI: Correlations with structure and function in an active enzyme
    • Mandel, A. M., Akke, M., and Palmer, A. G. (1995) Backbone dynamics of Escherichia coli ribonuclease HI: Correlations with structure and function in an active enzyme, J. Mol. Biol. 246, 144-163.
    • (1995) J. Mol. Biol. , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer, A.G.3
  • 79
    • 0024449503 scopus 로고
    • 15N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease
    • 15N 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.