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Volumn 46, Issue 8, 2007, Pages 2156-2173

A network of conserved interactions regulates the allosteric signal in a glutamine amidotransferase

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERIC TRANSITION; HINGE-OPENING MOTION; SUBSTRATE-BINDING SITE; UNDOCKING;

EID: 33847609615     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061708e     Document Type: Article
Times cited : (76)

References (69)
  • 1
    • 20344370764 scopus 로고    scopus 로고
    • Allosteric mechanisms of signal transduction
    • Changeux, J., and Edelstein, S. J. (2005) Allosteric mechanisms of signal transduction, Science 308, 1424-1428.
    • (2005) Science , vol.308 , pp. 1424-1428
    • Changeux, J.1    Edelstein, S.J.2
  • 2
    • 73649152457 scopus 로고
    • Allosteric proteins and cellular control systems
    • Monod, J., Changeux, J., and Jacob, F. (1963) Allosteric proteins and cellular control systems, J. Mol. Biol. 6, 306-329.
    • (1963) J. Mol. Biol , vol.6 , pp. 306-329
    • Monod, J.1    Changeux, J.2    Jacob, F.3
  • 3
    • 0030024963 scopus 로고    scopus 로고
    • The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families
    • Tesmer, J. J., Klem, T. J., Deras, M. L., Davisson, V. J., and Smith, J. L. (1996) The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families, Nat. Struct. Biol. 3, 74-86.
    • (1996) Nat. Struct. Biol , vol.3 , pp. 74-86
    • Tesmer, J.J.1    Klem, T.J.2    Deras, M.L.3    Davisson, V.J.4    Smith, J.L.5
  • 4
    • 0033594932 scopus 로고    scopus 로고
    • The Amidotransferase Family of Enzymes: Molecular Machines for the Production and Delivery of Ammonia
    • Raushel, F. M., Thoden, J. B., and Holden, H. M. (1999) The Amidotransferase Family of Enzymes: Molecular Machines for the Production and Delivery of Ammonia, Biochemistry 38, 7891-7899.
    • (1999) Biochemistry , vol.38 , pp. 7891-7899
    • Raushel, F.M.1    Thoden, J.B.2    Holden, H.M.3
  • 6
    • 0026643934 scopus 로고
    • ρ-Aminobenzoate Synthesis in Escherichia coli: Kinetic and Mechanistic Characterization of the Amidotransferase PabA
    • Roux, B., and Walsh, C. T. (1992) ρ-Aminobenzoate Synthesis in Escherichia coli: Kinetic and Mechanistic Characterization of the Amidotransferase PabA, Biochemistry 31, 6904-6910.
    • (1992) Biochemistry , vol.31 , pp. 6904-6910
    • Roux, B.1    Walsh, C.T.2
  • 7
    • 0025777753 scopus 로고
    • The catalytic mechanism of the amidotransferase domain of the syrian hamster multifunctional protein cad
    • Chaparian, M. G., and Evans, D. R. (1991) The catalytic mechanism of the amidotransferase domain of the syrian hamster multifunctional protein cad, J. Biol. Chem. 266, 3387-3395.
    • (1991) J. Biol. Chem , vol.266 , pp. 3387-3395
    • Chaparian, M.G.1    Evans, D.R.2
  • 8
    • 0037715142 scopus 로고    scopus 로고
    • Thr-431 and Arg-433 are part of a conserved sequence motif of the glutamine amidotransferase domain of CTP synthetases and are involved in GTP activation of Lactococcus lactis enzyme
    • Willemoes, M. (2003) Thr-431 and Arg-433 are part of a conserved sequence motif of the glutamine amidotransferase domain of CTP synthetases and are involved in GTP activation of Lactococcus lactis enzyme, J. Biol. Chem. 278, 9407-9411.
    • (2003) J. Biol. Chem , vol.278 , pp. 9407-9411
    • Willemoes, M.1
  • 9
    • 0028821816 scopus 로고
    • The glutamine hydrolysis function of human GMP synthetase
    • Nakamura, J., Straub, K., Wu, J., and Lou, L. (1995) The glutamine hydrolysis function of human GMP synthetase, J. Biol. Chem. 270, 23450-23455.
    • (1995) J. Biol. Chem , vol.270 , pp. 23450-23455
    • Nakamura, J.1    Straub, K.2    Wu, J.3    Lou, L.4
  • 11
    • 0034854997 scopus 로고    scopus 로고
    • Glutamine in animal science and production
    • Lobley, G. E., Hoskin, S. O., and McNeil, C. J. (2001) Glutamine in animal science and production, J. Nutr. 131, 2525S-2531S.
    • (2001) J. Nutr , vol.131
    • Lobley, G.E.1    Hoskin, S.O.2    McNeil, C.J.3
  • 12
    • 0028156367 scopus 로고
    • Regulation of cell function by the cellular hydration state
    • Haussinger, D., Lang, F., and Gerok, W. (1994) Regulation of cell function by the cellular hydration state, Am. J. Physio. 267, E343-E355.
    • (1994) Am. J. Physio , vol.267
    • Haussinger, D.1    Lang, F.2    Gerok, W.3
  • 13
    • 0037938734 scopus 로고    scopus 로고
    • Substrate-Induced Changes in the Ammonia Channel for Imidazole Glycerol Phosphate Synthase
    • Myers, R. S., Jensen, J., Deras, I., Smith, J. L., and Davisson, V. J. (2003) Substrate-Induced Changes in the Ammonia Channel for Imidazole Glycerol Phosphate Synthase, Biochemistry 42, 7013-7022.
    • (2003) Biochemistry , vol.42 , pp. 7013-7022
    • Myers, R.S.1    Jensen, J.2    Deras, I.3    Smith, J.L.4    Davisson, V.J.5
  • 14
    • 0038614879 scopus 로고    scopus 로고
    • Toward Understanding the Mechanism of the Complex Cyclization Reaction Catalyzed by Imidazole Glycerolphosphate Synthase: Crystal Structures of a Ternary Complex and the Free Enzyme
    • Chaudhuri, B. N., Lange, S. C., Myers, R. S., Davisson, V. J., and Smith, J. L. (2003) Toward Understanding the Mechanism of the Complex Cyclization Reaction Catalyzed by Imidazole Glycerolphosphate Synthase: Crystal Structures of a Ternary Complex and the Free Enzyme, Biochemistry 42, 7003-7012.
    • (2003) Biochemistry , vol.42 , pp. 7003-7012
    • Chaudhuri, B.N.1    Lange, S.C.2    Myers, R.S.3    Davisson, V.J.4    Smith, J.L.5
  • 16
    • 23244440559 scopus 로고    scopus 로고
    • Structural elements exclude water to optimize ammonia transfer in IGP synthase
    • Amaro, R. E., Myers, R. S., Davisson, V. J., and Luthey-Schulten, Z. A. (2005) Structural elements exclude water to optimize ammonia transfer in IGP synthase, Biophys. J. 89, 475-487.
    • (2005) Biophys. J , vol.89 , pp. 475-487
    • Amaro, R.E.1    Myers, R.S.2    Davisson, V.J.3    Luthey-Schulten, Z.A.4
  • 18
    • 23244441019 scopus 로고    scopus 로고
    • Reaction Coupling through Interdomain Contacts in Imidazole Glycerol Phosphate Synthase
    • Myers, R. S., Amaro, R. E., Luthey-Schulten, Z. A., and Davisson, V. J. (2005) Reaction Coupling through Interdomain Contacts in Imidazole Glycerol Phosphate Synthase, Biochemistry 44, 11974-11985.
    • (2005) Biochemistry , vol.44 , pp. 11974-11985
    • Myers, R.S.1    Amaro, R.E.2    Luthey-Schulten, Z.A.3    Davisson, V.J.4
  • 19
    • 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. (2002) Evolutionarily conserved networks of residues mediate allosteric communication in proteins, Nat. Struct. Mol. Bio. 10, 59-68.
    • (2002) Nat. Struct. Mol. Bio , vol.10 , pp. 59-68
    • Suel, G.M.1    Lockless, S.W.2    Wall, M.A.3    Ranganathan, R.4
  • 20
    • 17044427535 scopus 로고    scopus 로고
    • Network of dynamically important residues in the open/closed transition in polymerases is strongly conserved
    • Zheng, W., Brooks, B. R., Doniach, S., and Thirumalai, D. (2005) Network of dynamically important residues in the open/closed transition in polymerases is strongly conserved, Structure 13, 565-577.
    • (2005) Structure , vol.13 , pp. 565-577
    • Zheng, W.1    Brooks, B.R.2    Doniach, S.3    Thirumalai, D.4
  • 21
    • 0033534173 scopus 로고    scopus 로고
    • The Small Subunit of Carbamoyl Phosphate Synthetase: Snapshots along the Reaction Pathway
    • Thoden, J. B., Huang, X., Raushel, F. M., and Holden, H. M. (1999) The Small Subunit of Carbamoyl Phosphate Synthetase: Snapshots along the Reaction Pathway, Biochemistry 38, 16158-16166.
    • (1999) Biochemistry , vol.38 , pp. 16158-16166
    • Thoden, J.B.1    Huang, X.2    Raushel, F.M.3    Holden, H.M.4
  • 22
    • 0041784950 scopus 로고    scopus 로고
    • MacKerell, A. D., Jr., Bashford, D., Bellott, M., Dunbrack, R. L., Evanseck, J. D., Field, M. J., Fischer, S., Gao, J., Guo, H., Ha, S., Joseph-McCarthy, D., Kuchnir, L., Kuczera, K., Lau, F. T. K., Mattos, C., Michnick, S., Ngo, T., Nguyen, D. T., Prodhom, B., Reiher, W. E., III, Roux, B., Schlenkrich, M., Smith, J. C., Stote, R., Straub, J., Watanabe, M., Wiorkiewicz-Kuczera, J., Yin, D., and Karplus, M. (1998) All-Atom Empirical Potential for Molecular Modeling and Dynamics Studies of Proteins, J. Phys. Chem. B 102, 3586-3616.
    • MacKerell, A. D., Jr., Bashford, D., Bellott, M., Dunbrack, R. L., Evanseck, J. D., Field, M. J., Fischer, S., Gao, J., Guo, H., Ha, S., Joseph-McCarthy, D., Kuchnir, L., Kuczera, K., Lau, F. T. K., Mattos, C., Michnick, S., Ngo, T., Nguyen, D. T., Prodhom, B., Reiher, W. E., III, Roux, B., Schlenkrich, M., Smith, J. C., Stote, R., Straub, J., Watanabe, M., Wiorkiewicz-Kuczera, J., Yin, D., and Karplus, M. (1998) All-Atom Empirical Potential for Molecular Modeling and Dynamics Studies of Proteins, J. Phys. Chem. B 102, 3586-3616.
  • 25
    • 8644260166 scopus 로고    scopus 로고
    • Molecular dynamics simulations of substrate channeling though an alpha-beta barrel protein
    • Amaro, R., and Luthey-Schulten, Z. (2004) Molecular dynamics simulations of substrate channeling though an alpha-beta barrel protein, Chem. Phys. 307, 147-155.
    • (2004) Chem. Phys , vol.307 , pp. 147-155
    • Amaro, R.1    Luthey-Schulten, Z.2
  • 27
    • 33847635421 scopus 로고    scopus 로고
    • Grubmüller, H, 1996 Solvate, Theoretical Biophysics Group, Institute for Medical Optics, Ludwig-Maximilians University, Munich, Version 1.0
    • Grubmüller, H. (1996) Solvate, Theoretical Biophysics Group, Institute for Medical Optics, Ludwig-Maximilians University, Munich, Version 1.0.
  • 29
    • 36449007836 scopus 로고
    • Constant pressure molecular dynamics simulation: The Langevin piston method
    • Feller, S., Zhang, Z., Pastor, R., and Brooks, B. (1995) Constant pressure molecular dynamics simulation: The Langevin piston method, J. Chem. Phys. 103, 4613-4621.
    • (1995) J. Chem. Phys , vol.103 , pp. 4613-4621
    • Feller, S.1    Zhang, Z.2    Pastor, R.3    Brooks, B.4
  • 30
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N.log(N) method for Ewald sums in large systems
    • Darden, T., York, D., and Pedersen, L. (1993) Particle mesh Ewald: An N.log(N) method for Ewald sums in large systems, J. Chem. Phys. 98, 10089-10092.
    • (1993) J. Chem. Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 31
    • 84963146276 scopus 로고    scopus 로고
    • Grubmüller, H., Heller, H., Windemuth, A., and Schulten, K. (1991) Generalized Verlet algorithm for efficient molecular dynamics simulations with long-range interactions, Mol. Simul. 6, 121-142.
    • Grubmüller, H., Heller, H., Windemuth, A., and Schulten, K. (1991) Generalized Verlet algorithm for efficient molecular dynamics simulations with long-range interactions, Mol. Simul. 6, 121-142.
  • 32
    • 85190253182 scopus 로고    scopus 로고
    • Schlick, T., Skeel, R., Brunger, A., Kale, L., Board, J. A., Hermans, J., and Schulten, K. (1999) Algorithmic challenges in computational molecular biophysics, J. Comp. Phys. 151, 9-48.
    • Schlick, T., Skeel, R., Brunger, A., Kale, L., Board, J. A., Hermans, J., and Schulten, K. (1999) Algorithmic challenges in computational molecular biophysics, J. Comp. Phys. 151, 9-48.
  • 36
    • 0033573912 scopus 로고    scopus 로고
    • Forced unfolding of fibronectin type III module reveals a tensile molecular recognition switch
    • Krammer, A., Lu, H., Isralewitz, B., Schulten, K., and Vogel, V. (1999) Forced unfolding of fibronectin type III module reveals a tensile molecular recognition switch, Proc. Natl. Acad. Sci. U.S.A. 96, 1351-1356.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 1351-1356
    • Krammer, A.1    Lu, H.2    Isralewitz, B.3    Schulten, K.4    Vogel, V.5
  • 37
    • 0344736695 scopus 로고    scopus 로고
    • Structural and functional significance of mechanically unfolded fibronectin type III intermediates
    • Gao, M., Craig, D., Lequin, O., Campbell, I., Vogel, V., and Schulten, K. (2003) Structural and functional significance of mechanically unfolded fibronectin type III intermediates, Proc. Natl. Acad. Sci. U.S.A. 100, 14784-14789.
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 14784-14789
    • Gao, M.1    Craig, D.2    Lequin, O.3    Campbell, I.4    Vogel, V.5    Schulten, K.6
  • 40
    • 4244116139 scopus 로고    scopus 로고
    • Equilibrium free-energy differences from nonequilibrium measurements: A master-equation approach
    • Jarzynski, C. (1997) Equilibrium free-energy differences from nonequilibrium measurements: A master-equation approach, Phys. Rev. E 56, 5018-5035.
    • (1997) Phys. Rev. E , vol.56 , pp. 5018-5035
    • Jarzynski, C.1
  • 41
    • 4243754128 scopus 로고    scopus 로고
    • Nonequilibrium equality for free energy differences
    • Jarzynski, C. (1997) Nonequilibrium equality for free energy differences, Phys. Rev. Lett. 78, 2690-2693.
    • (1997) Phys. Rev. Lett , vol.78 , pp. 2690-2693
    • Jarzynski, C.1
  • 42
    • 0042885340 scopus 로고    scopus 로고
    • Free energy calculation from steered molecular dynamics simulations using Jarzynski's identity
    • Park, S., Khalili-Araghi, F., Tajkhorshid, E., and Schulten, K. (2003) Free energy calculation from steered molecular dynamics simulations using Jarzynski's identity, J. Chem. Phys. 119, 3559-3566.
    • (2003) J. Chem. Phys , vol.119 , pp. 3559-3566
    • Park, S.1    Khalili-Araghi, F.2    Tajkhorshid, E.3    Schulten, K.4
  • 43
    • 0000577041 scopus 로고
    • Large-amplitude nonlinear motions in proteins
    • Garcia, A. E. (1992) Large-amplitude nonlinear motions in proteins, Phys. Rev. Lett. 68, 2696-2699.
    • (1992) Phys. Rev. Lett , vol.68 , pp. 2696-2699
    • Garcia, A.E.1
  • 44
    • 0028292635 scopus 로고
    • Harmonic and anharmonic aspects in the dynamics of BPTI: A normal mode analysis and principal component analysis
    • Hayward, S., Kitao, A., and Go, N. (1994) Harmonic and anharmonic aspects in the dynamics of BPTI: a normal mode analysis and principal component analysis, Protein Sci. 3, 936-943.
    • (1994) Protein Sci , vol.3 , pp. 936-943
    • Hayward, S.1    Kitao, A.2    Go, N.3
  • 45
    • 0001295503 scopus 로고    scopus 로고
    • Principal component analysis and long time protein dynamics
    • Balsera, M. A., Wriggers, W., Oono, Y., and Schulten, K. (1996) Principal component analysis and long time protein dynamics, J. Phys. Chem. 100, 2567-2572.
    • (1996) J. Phys. Chem , vol.100 , pp. 2567-2572
    • Balsera, M.A.1    Wriggers, W.2    Oono, Y.3    Schulten, K.4
  • 46
    • 0031910020 scopus 로고    scopus 로고
    • Locally accessible conformations of proteins: Multiple molecular dynamics simulations of crambin
    • Caves, L. S. D., Evanseck, J. D., and Karplus, M. (1998) Locally accessible conformations of proteins: multiple molecular dynamics simulations of crambin, Protein Sci. 7, 649-666.
    • (1998) Protein Sci , vol.7 , pp. 649-666
    • Caves, L.S.D.1    Evanseck, J.D.2    Karplus, M.3
  • 47
    • 0034906622 scopus 로고    scopus 로고
    • Analysis of a 10-ns molecular dynamics simulation of mouse acetylcholinesterase
    • Tai, K., Shen, T., Börjesson, U., Philppopoulos, M., and McCammon, J. A. (2001) Analysis of a 10-ns molecular dynamics simulation of mouse acetylcholinesterase, Biophys. J. 81, 715-724.
    • (2001) Biophys. J , vol.81 , pp. 715-724
    • Tai, K.1    Shen, T.2    Börjesson, U.3    Philppopoulos, M.4    McCammon, J.A.5
  • 48
    • 33749442647 scopus 로고    scopus 로고
    • Multiseq: Unifying sequence and structure data for evolutionary analysis
    • Eargle, J., Roberts, E., Wright, D., and Luthey-Schulten, Z. (2006) Multiseq: unifying sequence and structure data for evolutionary analysis. BMC Bioinformatics 7, 382.
    • (2006) BMC Bioinformatics , vol.7 , pp. 382
    • Eargle, J.1    Roberts, E.2    Wright, D.3    Luthey-Schulten, Z.4
  • 49
    • 0026743174 scopus 로고
    • Multiple protein sequence alignment from tertiary structure comparison: Assignment of global and residue confidence levels
    • Russel, R. B., and Barton, G. J. (1992) Multiple protein sequence alignment from tertiary structure comparison: Assignment of global and residue confidence levels, Proteins: Struc., Funct., Genet. 14, 309-323.
    • (1992) Proteins: Struc., Funct., Genet , vol.14 , pp. 309-323
    • Russel, R.B.1    Barton, G.J.2
  • 50
    • 0035327183 scopus 로고    scopus 로고
    • Evaluating protein structure-prediction schemes using energy landscape theory
    • Eastwood, M. P., Hardin, C., Luthey-Schulten, Z., and Wolynes, P. G. (2001) Evaluating protein structure-prediction schemes using energy landscape theory, IBM J. Res. Dev. 45, 475-497.
    • (2001) IBM J. Res. Dev , vol.45 , pp. 475-497
    • Eastwood, M.P.1    Hardin, C.2    Luthey-Schulten, Z.3    Wolynes, P.G.4
  • 51
    • 0026076090 scopus 로고
    • Collective motions in proteins: A covariance analysis of atomic fluctuations in molecular dynamics and normal mode simulations
    • Ichiye, T., and Karplus, M. (1991) Collective motions in proteins: a covariance analysis of atomic fluctuations in molecular dynamics and normal mode simulations, Proteins: Struc., Funct., Genet. 11, 205-217.
    • (1991) Proteins: Struc., Funct., Genet , vol.11 , pp. 205-217
    • Ichiye, T.1    Karplus, M.2
  • 52
    • 0029092698 scopus 로고
    • Fluctuation and cross-correlation analysis of protein motions observed in nanosecond molecular dynamics simulations
    • Hünenberger, P. H., Mark, A. E., and van Gunsteren, W. F. (1995) Fluctuation and cross-correlation analysis of protein motions observed in nanosecond molecular dynamics simulations, J. Mol. Biol. 252, 492-503.
    • (1995) J. Mol. Biol , vol.252 , pp. 492-503
    • Hünenberger, P.H.1    Mark, A.E.2    van Gunsteren, W.F.3
  • 53
    • 0035815288 scopus 로고    scopus 로고
    • Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation
    • Young, M. A., Gongloni, S., Superti-Furga, G., Roux, B., and Kuriyan, J. (2001) Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation, Cell 105, 115-126.
    • (2001) Cell , vol.105 , pp. 115-126
    • Young, M.A.1    Gongloni, S.2    Superti-Furga, G.3    Roux, B.4    Kuriyan, J.5
  • 55
    • 0033621118 scopus 로고    scopus 로고
    • The propagation of binding interactions to remote sites in proteins: Analysis of the binding of the monoclonal antibody D1.3 to lysozyme
    • Freire, E. (1999) The propagation of binding interactions to remote sites in proteins: Analysis of the binding of the monoclonal antibody D1.3 to lysozyme, Proc. Natl. Acad. Sci. U.S.A. 96, 10118-10122.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 10118-10122
    • Freire, E.1
  • 56
    • 0033642945 scopus 로고    scopus 로고
    • Structural stability of binding sites: Consequences for binding affinity and allosteric effects
    • Luque, I., and Freire, E. (2000) Structural stability of binding sites: Consequences for binding affinity and allosteric effects, Proteins: Struc., Funct., and Gen. 41, 63-71.
    • (2000) Proteins: Struc., Funct., and Gen , vol.41 , pp. 63-71
    • Luque, I.1    Freire, E.2
  • 57
    • 0034255123 scopus 로고    scopus 로고
    • Shoemaker, B., Portman, J., and Wolynes, P. (2000) Speeding molecular recognition by using the folding funnel: The fly-casting mechanism, PNAS 97, 8868-8873.
    • Shoemaker, B., Portman, J., and Wolynes, P. (2000) Speeding molecular recognition by using the folding funnel: The fly-casting mechanism, PNAS 97, 8868-8873.
  • 58
    • 0035967856 scopus 로고    scopus 로고
    • Solution-state nmr investigations of triosephosphate isomerase active site loop motion: Ligand release in relation to active site loop dynamics
    • Rozovsky, S., Jogl, G., Tong, L., and McDermott, A. E. (2001) Solution-state nmr investigations of triosephosphate isomerase active site loop motion: Ligand release in relation to active site loop dynamics, J. Mol. Biol. 310, 271-280.
    • (2001) J. Mol. Biol , vol.310 , pp. 271-280
    • Rozovsky, S.1    Jogl, G.2    Tong, L.3    McDermott, A.E.4
  • 59
    • 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
  • 61
    • 0033812585 scopus 로고    scopus 로고
    • Identifying conformational changes with site-directed spin labeling
    • Hubbell, W. L., Cafiso, D. S., and Altenbach, C. (2000) Identifying conformational changes with site-directed spin labeling, Nat. Struct. Biol. 7, 735-739.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 735-739
    • Hubbell, W.L.1    Cafiso, D.S.2    Altenbach, C.3
  • 62
    • 0032574827 scopus 로고    scopus 로고
    • Dynamics and function of proteins: The search for general concepts
    • Frauenfelder, H., and McMahon, B. (1998) Dynamics and function of proteins: the search for general concepts, Proc. Natl. Acad. Sci. U.S.A. 95, 4795-4797.
    • (1998) Proc. Natl. Acad. Sci. U.S.A , vol.95 , pp. 4795-4797
    • Frauenfelder, H.1    McMahon, B.2
  • 64
    • 0020771265 scopus 로고
    • Dynamics of a small protein in terms of low-frequency vibrational modes
    • Go, N., Noguti, T., and Nishikawa, T. (1983) Dynamics of a small protein in terms of low-frequency vibrational modes, Proc. Natl. Acad. Sci. U.S.A. 80, 3696-3670.
    • (1983) Proc. Natl. Acad. Sci. U.S.A , vol.80 , pp. 3696-3670
    • Go, N.1    Noguti, T.2    Nishikawa, T.3
  • 65
    • 84990678054 scopus 로고
    • The normal modes of a protein: Native bovine pancreatic trypsin inhibitor
    • Levitt, M., Sander, C., and Stern, P. S. (1983) The normal modes of a protein: native bovine pancreatic trypsin inhibitor, Int. J. Quant. Chem. 10, 181-199.
    • (1983) Int. J. Quant. Chem , vol.10 , pp. 181-199
    • Levitt, M.1    Sander, C.2    Stern, P.S.3
  • 66
    • 0030623823 scopus 로고    scopus 로고
    • Direct evaluation of thermal fluctuations using a single parameter harmonic potential
    • Bahar, I., Atilgan, A. R., and Erman, B. (1997) Direct evaluation of thermal fluctuations using a single parameter harmonic potential, Folding, Des. 2, 173-181.
    • (1997) Folding, Des , vol.2 , pp. 173-181
    • Bahar, I.1    Atilgan, A.R.2    Erman, B.3
  • 67
    • 0034308140 scopus 로고    scopus 로고
    • Building-block approach for determining low-frequency normal modes of macromolecules
    • Tama, F., Gadea, F. X., Marques, O., and Sanejouand, Y. H. (2000) Building-block approach for determining low-frequency normal modes of macromolecules, Proteins: Struct., Funct., Genet. 41, 1-7.
    • (2000) Proteins: Struct., Funct., Genet , vol.41 , pp. 1-7
    • Tama, F.1    Gadea, F.X.2    Marques, O.3    Sanejouand, Y.H.4
  • 68
    • 25844431698 scopus 로고    scopus 로고
    • Coarse-grained normal mode analysis in structural biology
    • Bahar, I., and Rader, A. J. (2005) Coarse-grained normal mode analysis in structural biology, Curr. Opin. Struct. Biol. 15, 586-592.
    • (2005) Curr. Opin. Struct. Biol , vol.15 , pp. 586-592
    • Bahar, I.1    Rader, A.J.2
  • 69
    • 3242875210 scopus 로고    scopus 로고
    • Elnemo: A normal mode web-server for protein movement analysis and the generation of templates for molecular replacement
    • Suhre, K., and Sanejouand, Y. H. (2004) Elnemo: a normal mode web-server for protein movement analysis and the generation of templates for molecular replacement, Nucl. Acids Res. 32, W610-W614.
    • (2004) Nucl. Acids Res , vol.32
    • Suhre, K.1    Sanejouand, Y.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.