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Volumn 56, Issue 3, 2004, Pages 449-463

Cis/trans isomerization in HIV-1 capsid protein catalyzed by cyclophilin A: Insights from computational and theoretical studies

Author keywords

Enzymatic catalysis; Enzyme catalysis; Isomerase; Peptidyl prolyl cis trans isomerase activity; Protein dynamics; Protein protein interaction; Vibrations network

Indexed keywords

CAPSID PROTEIN; CYCLOPHILIN A;

EID: 3142661685     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20135     Document Type: Article
Times cited : (55)

References (67)
  • 1
    • 0028049327 scopus 로고
    • Dynamics of a flexible loop in dihydrofolate reductase from Escherichia coli and its implication for catalysis
    • Falzone CJ, Wright PE, Benkovic SJ. Dynamics of a flexible loop in dihydrofolate reductase from Escherichia coli and its implication for catalysis. Biochemistry 1994;33:439-442.
    • (1994) Biochemistry , vol.33 , pp. 439-442
    • Falzone, C.J.1    Wright, P.E.2    Benkovic, S.J.3
  • 2
    • 0029102089 scopus 로고
    • Dynamics of the dihydrofolate reductase-folate complex: Catalytic sites and regions known to undergo conformational change exhibit diverse dynamical features
    • Epstein DM, Benkovic SJ, Wright PE. Dynamics of the dihydrofolate reductase-folate complex: catalytic sites and regions known to undergo conformational change exhibit diverse dynamical features. Biochemistry 1995;34:11037-11048.
    • (1995) Biochemistry , vol.34 , pp. 11037-11048
    • Epstein, D.M.1    Benkovic, S.J.2    Wright, P.E.3
  • 3
    • 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 CE, Benkovic SJ. 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 1997;36:15792-15800.
    • (1997) Biochemistry , vol.36 , pp. 15792-15800
    • Cameron, C.E.1    Benkovic, S.J.2
  • 4
    • 0035928796 scopus 로고    scopus 로고
    • Backbone dynamics in dihydrofolate reductase complexes: Role of loop flexibility in the catalytic mechanism
    • Osborne MJ, Schnell J, Benkovic SJ, Dyson HJ, Wright PE. Backbone dynamics in dihydrofolate reductase complexes: role of loop flexibility in the catalytic mechanism. Biochemistry 2001;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
  • 7
    • 0037076522 scopus 로고    scopus 로고
    • Evidence for flexibility in the function of ribonuclease A
    • Cole R, Loria JP. Evidence for flexibility in the function of ribonuclease A. Biochemistry 2002;41:6072-6081.
    • (2002) Biochemistry , vol.41 , pp. 6072-6081
    • Cole, R.1    Loria, J.P.2
  • 8
    • 0034636990 scopus 로고    scopus 로고
    • A view of dynamics changes in the molten globule native folding step by quasielastic neutron scattering
    • Bu ZM, Neumann DA, Lee SH, Brown CM, Engelman DM, Han CC. A view of dynamics changes in the molten globule native folding step by quasielastic neutron scattering. J Mol Biol 2000;301:525-536.
    • (2000) J Mol Biol , vol.301 , pp. 525-536
    • Bu, Z.M.1    Neumann, D.A.2    Lee, S.H.3    Brown, C.M.4    Engelman, D.M.5    Han, C.C.6
  • 9
    • 0035807881 scopus 로고    scopus 로고
    • Fast dynamics of halophilic malate dehydrogenase and BSA measured by neutron scattering under various solvent conditions influencing protein stability
    • Tehei M, Madern D, Pfister C, Zaccai G. Fast dynamics of halophilic malate dehydrogenase and BSA measured by neutron scattering under various solvent conditions influencing protein stability. Proc Natl Acad Sci USA 2001;98:14356-14361.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14356-14361
    • Tehei, M.1    Madern, D.2    Pfister, C.3    Zaccai, G.4
  • 11
    • 0037137214 scopus 로고    scopus 로고
    • Temperature dependence of the internal dynamics of a calmodulin-peptide complex
    • Lee AL, Sharp KA, Kranz JK, Song XJ, Wand AJ. Temperature dependence of the internal dynamics of a calmodulin-peptide complex. Biochemistry 2002;41:13814-13825.
    • (2002) Biochemistry , vol.41 , pp. 13814-13825
    • Lee, A.L.1    Sharp, K.A.2    Kranz, J.K.3    Song, X.J.4    Wand, A.J.5
  • 12
    • 0029000872 scopus 로고
    • Dynamics of the flexible loop of triosephosphate isomerase: The loop motion is not ligand gated
    • Williams JC, McDermott AE. Dynamics of the flexible loop of triosephosphate isomerase: the loop motion is not ligand gated. Biochemistry 1995;34:8309-8319.
    • (1995) Biochemistry , vol.34 , pp. 8309-8319
    • Williams, J.C.1    McDermott, A.E.2
  • 13
    • 0034724392 scopus 로고    scopus 로고
    • Millisecond time scale conformational flexibility in a hyperthermophile protein at ambient temperature
    • Hernandez G, Jenney FE, Adams MWW, LeMaster DM. Millisecond time scale conformational flexibility in a hyperthermophile protein at ambient temperature. Proc Natl Acad Sci USA 2000;97:3166-3170.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3166-3170
    • Hernandez, G.1    Jenney, F.E.2    Adams, M.W.W.3    LeMaster, D.M.4
  • 14
    • 0032560505 scopus 로고    scopus 로고
    • Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins
    • Zavodszky P, Kardos J, Svingor A, Petsko GA. Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins. Proc Natl Acad Sci USA 1998;95:7406-7411.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7406-7411
    • Zavodszky, P.1    Kardos, J.2    Svingor, A.3    Petsko, G.A.4
  • 16
    • 0025331920 scopus 로고
    • Crystallographic analysis of the complex between triosephosphate isomerase and 2 phosphoglycolate at 2.5-A resolution: Implications for catalysis
    • Lolis E, Petsko GA. Crystallographic analysis of the complex between triosephosphate isomerase and 2 phosphoglycolate at 2.5-A resolution: implications for catalysis. Biochemistry 1990;29:6619-6625.
    • (1990) Biochemistry , vol.29 , pp. 6619-6625
    • Lolis, E.1    Petsko, G.A.2
  • 17
    • 0031015737 scopus 로고    scopus 로고
    • Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence
    • Sawaya MR, Kraut J. Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. Biochemistry 1997;36:586-603.
    • (1997) Biochemistry , vol.36 , pp. 586-603
    • Sawaya, M.R.1    Kraut, J.2
  • 18
    • 0030877587 scopus 로고    scopus 로고
    • Conformational substates in enzyme mechanism: The 120 K structure of α-lytic protease at 1.5 Å resolution
    • Rader SD, Agard DA. Conformational substates in enzyme mechanism: the 120 K structure of α-lytic protease at 1.5 Å resolution. Protein Sci 1997;6:1375-1386.
    • (1997) Protein Sci , vol.6 , pp. 1375-1386
    • Rader, S.D.1    Agard, D.A.2
  • 19
    • 0033955055 scopus 로고    scopus 로고
    • Protein dynamics in enzymatic catalysis: Exploration of dihydrofolate reductase
    • Radkiewicz JL, Brooks CL. Protein dynamics in enzymatic catalysis: exploration of dihydrofolate reductase. J Am Chem Soc 2000;122:225-231.
    • (2000) J Am Chem Soc , vol.122 , pp. 225-231
    • Radkiewicz, J.L.1    Brooks, C.L.2
  • 20
    • 0037012441 scopus 로고    scopus 로고
    • Identification of a protein-promoting vibration in the reaction catalyzed by horse liver alcohol dehydrogenase
    • Caratzoulas S, Mincer JS, Schwartz SD. Identification of a protein-promoting vibration in the reaction catalyzed by horse liver alcohol dehydrogenase. J Am Chem Soc 2002;124:3270-3276.
    • (2002) J Am Chem Soc , vol.124 , pp. 3270-3276
    • Caratzoulas, S.1    Mincer, J.S.2    Schwartz, S.D.3
  • 22
    • 0037188007 scopus 로고    scopus 로고
    • Nuclear quantum effects and enzyme dynamics in dihydrofolate reductase catalysis
    • Agarwal PK, Billeter SR, Hammes-Schiffer S. Nuclear quantum effects and enzyme dynamics in dihydrofolate reductase catalysis. J Phys Chem B 2002;106:3283-3293.
    • (2002) J Phys Chem B , vol.106 , pp. 3283-3293
    • Agarwal, P.K.1    Billeter, S.R.2    Hammes-Schiffer, S.3
  • 23
    • 0344391945 scopus 로고    scopus 로고
    • Reaction-path energetics and kinetics of the hydride transfer reaction catalyzed by dihydrofolate reductase
    • Garcia-Viloca M, Truhlar DG, Gao JL. Reaction-path energetics and kinetics of the hydride transfer reaction catalyzed by dihydrofolate reductase. Biochemistry 2003;42:13558-13575.
    • (2003) Biochemistry , vol.42 , pp. 13558-13575
    • Garcia-Viloca, M.1    Truhlar, D.G.2    Gao, J.L.3
  • 25
    • 0021159379 scopus 로고
    • Cyclophilin: A specific cytosolic binding protein for cyclosporin A
    • Handschumacher RE, Harding MW, Rice J, Drugge RJ. Cyclophilin: a specific cytosolic binding protein for cyclosporin A. Science 1984;226:544-547.
    • (1984) Science , vol.226 , pp. 544-547
    • Handschumacher, R.E.1    Harding, M.W.2    Rice, J.3    Drugge, R.J.4
  • 26
    • 0024959451 scopus 로고
    • Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin
    • Takahashi N, Hayano T, Suzuki M. Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin. Nature 1989;337:473-475.
    • (1989) Nature , vol.337 , pp. 473-475
    • Takahashi, N.1    Hayano, T.2    Suzuki, M.3
  • 27
    • 0032926319 scopus 로고    scopus 로고
    • Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts
    • Gothel SF, Marahiel MA. Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts. Cell Mol Life Sci 1999;55:423-436.
    • (1999) Cell Mol Life Sci , vol.55 , pp. 423-436
    • Gothel, S.F.1    Marahiel, M.A.2
  • 28
    • 0034129915 scopus 로고    scopus 로고
    • The impact of immunosuppressive drugs on the analysis of T cell activation
    • Rovira P, Mascarell L, Truffa-Bachi P. The impact of immunosuppressive drugs on the analysis of T cell activation. Curr Med Chem 2000;7:673-692.
    • (2000) Curr Med Chem , vol.7 , pp. 673-692
    • Rovira, P.1    Mascarell, L.2    Truffa-Bachi, P.3
  • 29
    • 0034419296 scopus 로고    scopus 로고
    • Chemical aspects of peptide bond isomerisation
    • Fischer G. Chemical aspects of peptide bond isomerisation. Chem Soc Rev 2000;29:119-127.
    • (2000) Chem Soc Rev , vol.29 , pp. 119-127
    • Fischer, G.1
  • 32
    • 0036168738 scopus 로고    scopus 로고
    • trans-complementation rescue of cyclophilin A-deficient viruses reveals that the requirement for cyclophilin A in human immunodeficiency virus type 1 replication is independent of its isomerase activity
    • Saphire ACS, Bobardt MD, Gallay PA. trans-Complementation rescue of cyclophilin A-deficient viruses reveals that the requirement for cyclophilin A in human immunodeficiency virus type 1 replication is independent of its isomerase activity. J Virol 2002;76:2255-2262.
    • (2002) J Virol , vol.76 , pp. 2255-2262
    • Saphire, A.C.S.1    Bobardt, M.D.2    Gallay, P.A.3
  • 34
    • 0029887104 scopus 로고    scopus 로고
    • Cyclophilin A is required for the replication of group M human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus SIV(CPZ) GAB but not group O HIV-1 or other primate immunodeficiency viruses
    • Braaten D, Franke EK, Luban J. Cyclophilin A is required for the replication of group M human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus SIV(CPZ) GAB but not group O HIV-1 or other primate immunodeficiency viruses. J Virol 1996;70:4220-4227.
    • (1996) J Virol , vol.70 , pp. 4220-4227
    • Braaten, D.1    Franke, E.K.2    Luban, J.3
  • 35
    • 0036061001 scopus 로고    scopus 로고
    • Differential dependence of the infectivity of HIV-1 group O isolates on the cellular protein cyclophilin A
    • Wiegers K, Krausslich HG. Differential dependence of the infectivity of HIV-1 group O isolates on the cellular protein cyclophilin A. Virology 2002;294:289-295.
    • (2002) Virology , vol.294 , pp. 289-295
    • Wiegers, K.1    Krausslich, H.G.2
  • 36
    • 0027940713 scopus 로고
    • Specific incorporation of cyclophilin A into HIV-1 virions
    • Franke EK, Yuan HEH, Luban J. Specific incorporation of cyclophilin A into HIV-1 virions. Nature 1994;372:359-362.
    • (1994) Nature , vol.372 , pp. 359-362
    • Franke, E.K.1    Yuan, H.E.H.2    Luban, J.3
  • 38
    • 0029633186 scopus 로고
    • AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules
    • Pearlman DA, Case DA, Caldwell JW, Ross WS, Cheatham TE, Debolt S, Ferguson D, Seibel G, Kollman P. AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules. Comput Phys Commun 1995;91:1-41.
    • (1995) Comput Phys Commun , vol.91 , pp. 1-41
    • Pearlman, D.A.1    Case, D.A.2    Caldwell, J.W.3    Ross, W.S.4    Cheatham, T.E.5    Debolt, S.6    Ferguson, D.7    Seibel, G.8    Kollman, P.9
  • 41
    • 36749107785 scopus 로고
    • Molecular dynamics simulations at constant pressure and/or temperature
    • Andersen HC. Molecular dynamics simulations at constant pressure and/or temperature. J Chem Phys 1980;72:2384-2393.
    • (1980) J Chem Phys , vol.72 , pp. 2384-2393
    • Andersen, H.C.1
  • 42
    • 33646940952 scopus 로고
    • Numerical integration of Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert JP, Ciccotti G, Berendsen HJC. Numerical integration of Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J Comput Phys 1977;23:327-341.
    • (1977) J Comput Phys , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 44
    • 0342929614 scopus 로고
    • Nonphysical sampling distributions in Monte-Carlo free-energy estimation: Umbrella sampling
    • Torrie GM, Valleau JP. Nonphysical sampling distributions in Monte-Carlo free-energy estimation: umbrella sampling. J Comput Phys 1977;23:187-199.
    • (1977) J Comput Phys , vol.23 , pp. 187-199
    • Torrie, G.M.1    Valleau, J.P.2
  • 46
    • 0036025446 scopus 로고    scopus 로고
    • Quantum mechanical methods for enzyme kinetics
    • Gao JL, Truhlar DG. Quantum mechanical methods for enzyme kinetics. Annu Rev Phys Chem 2002;53:467-505.
    • (2002) Annu Rev Phys Chem , vol.53 , pp. 467-505
    • Gao, J.L.1    Truhlar, D.G.2
  • 47
    • 84986519238 scopus 로고
    • The weighted histogram analysis method for free-energy calculations on biomolecules. 1. The method
    • Kumar S, Bouzida D, Swendsen RH, Kollman PA, Rosenberg JM. The weighted histogram analysis method for free-energy calculations on biomolecules. 1. The method. J Comput Chem 1992;13:1011-1021.
    • (1992) J Comput Chem , vol.13 , pp. 1011-1021
    • Kumar, S.1    Bouzida, D.2    Swendsen, R.H.3    Kollman, P.A.4    Rosenberg, J.M.5
  • 48
    • 0000764091 scopus 로고
    • Constant temperature free energy surfaces for physical and chemical processes
    • Boczko EM, Brooks CL. Constant temperature free energy surfaces for physical and chemical processes. J Phys Chem 1993;97:4509-4513.
    • (1993) J Phys Chem , vol.97 , pp. 4509-4513
    • Boczko, E.M.1    Brooks, C.L.2
  • 49
    • 0000092491 scopus 로고
    • Promotion of helix formation in peptides dissolved in alcohol and water-alcohol mixtures
    • Brooks CL, Nilsson L. Promotion of helix formation in peptides dissolved in alcohol and water-alcohol mixtures. J Am Chem Soc 1993;115:11034-11035.
    • (1993) J Am Chem Soc , vol.115 , pp. 11034-11035
    • Brooks, C.L.1    Nilsson, L.2
  • 50
    • 0141459794 scopus 로고    scopus 로고
    • Free energy surface, reaction paths, and kinetic isotope effect of short-chain acyl-CoA dehydrogenase
    • Poulsen TD, Garcia-Viloca M, Gao JL, Truhlar DG. Free energy surface, reaction paths, and kinetic isotope effect of short-chain acyl-CoA dehydrogenase. J Phys Chem B 2003;107:9567-9578.
    • (2003) J Phys Chem B , vol.107 , pp. 9567-9578
    • Poulsen, T.D.1    Garcia-Viloca, M.2    Gao, J.L.3    Truhlar, D.G.4
  • 51
    • 0032996356 scopus 로고    scopus 로고
    • Simulation analysis of the retinal conformational equilibrium in dark adapted bacteriorhodopsin
    • Baudry J, Crouzy S, Roux B, Smith JC. Simulation analysis of the retinal conformational equilibrium in dark adapted bacteriorhodopsin. Biophys J 1999;76:1909-1917.
    • (1999) Biophys J , vol.76 , pp. 1909-1917
    • Baudry, J.1    Crouzy, S.2    Roux, B.3    Smith, J.C.4
  • 52
    • 0022419152 scopus 로고
    • Protein normal-mode dynamics: Trypsin inhibitor, crambin, ribonuclease and lysozyme
    • Levitt M, Sander C, Stern PS. Protein normal-mode dynamics: trypsin inhibitor, crambin, ribonuclease and lysozyme. J Mol Biol 1985;181:423-447.
    • (1985) J Mol Biol , vol.181 , pp. 423-447
    • Levitt, M.1    Sander, C.2    Stern, P.S.3
  • 54
    • 0000561283 scopus 로고
    • Investigation of domain structure in proteins via molecular dynamics simulation: Application to HIV-1 protease dimer
    • Swaminathan S, Harte WE, Beveridge DL. Investigation of domain structure in proteins via molecular dynamics simulation: application to HIV-1 protease dimer. J Am Chem Soc 1991;113:2717-2721.
    • (1991) J Am Chem Soc , vol.113 , pp. 2717-2721
    • Swaminathan, S.1    Harte, W.E.2    Beveridge, D.L.3
  • 55
    • 0000961995 scopus 로고
    • Evaluation of the configurational entropy for proteins: Application to molecular dynamics simulations ofan a-helix
    • Levy RM, Karplus M, Kushick J, Perahia D. Evaluation of the configurational entropy for proteins: application to molecular dynamics simulations ofan a-helix. Macromolecules 1984;17:1370-1374.
    • (1984) Macromolecules , vol.17 , pp. 1370-1374
    • Levy, R.M.1    Karplus, M.2    Kushick, J.3    Perahia, D.4
  • 56
    • 0000118827 scopus 로고
    • Harmonic and quasiharmonic descriptions of crambin
    • Teeter MM, Case DA. Harmonic and quasiharmonic descriptions of crambin. J Phys Chem 1990;94:8091-8097.
    • (1990) J Phys Chem , vol.94 , pp. 8091-8097
    • Teeter, M.M.1    Case, D.A.2
  • 57
    • 0001205818 scopus 로고
    • Electrostatic effects in water accessible regions of proteins
    • Mehler EL, Eichele G. Electrostatic effects in water accessible regions of proteins. Biochemistry 1984;23:3887-3891.
    • (1984) Biochemistry , vol.23 , pp. 3887-3891
    • Mehler, E.L.1    Eichele, G.2
  • 58
    • 0026332547 scopus 로고
    • Electrostatic effects in proteins: Comparison of dielectric and charge models
    • Mehler EL, Solmajer T. Electrostatic effects in proteins: comparison of dielectric and charge models. Protein Eng 1991;4:903-910.
    • (1991) Protein Eng , vol.4 , pp. 903-910
    • Mehler, E.L.1    Solmajer, T.2
  • 59
    • 0025035782 scopus 로고
    • Substrate specificity for the human rotamase FKBP: A view of FK506 and rapamycin as leucine-(twisted amide) proline mimics
    • Albers MW, Walsh CT, Schreiber SL. Substrate specificity for the human rotamase FKBP: a view of FK506 and rapamycin as leucine-(twisted amide) proline mimics. J Org Chem 1990;55:4984-4986.
    • (1990) J Org Chem , vol.55 , pp. 4984-4986
    • Albers, M.W.1    Walsh, C.T.2    Schreiber, S.L.3
  • 60
    • 0025373627 scopus 로고
    • Substrate specificities of the peptidyl prolyl cis-trans isomerase activities of cyclophilin and FK-506 binding-protein: Evidence for the existence of a family of distinct enzymes
    • Harrison RK, Stein RL. Substrate specificities of the peptidyl prolyl cis-trans isomerase activities of cyclophilin and FK-506 binding-protein: evidence for the existence of a family of distinct enzymes. Biochemistry 1990;29:3813-3816.
    • (1990) Biochemistry , vol.29 , pp. 3813-3816
    • Harrison, R.K.1    Stein, R.L.2
  • 61
    • 0025868143 scopus 로고
    • Determination of kinetic constants for peptidyl prolyl cis-trans isomerases by an improved spectrophotometric assay
    • Kofron JL, Kuzmic P, Kishore V, Colonbonilla E, Rich DH. Determination of kinetic constants for peptidyl prolyl cis-trans isomerases by an improved spectrophotometric assay. Biochemistry 1991;30:6127-6134.
    • (1991) Biochemistry , vol.30 , pp. 6127-6134
    • Kofron, J.L.1    Kuzmic, P.2    Kishore, V.3    Colonbonilla, E.4    Rich, D.H.5
  • 62
    • 0028877264 scopus 로고
    • Kinetic analysis of cyclophilin-catalyzed prolyl cis/trans isomerization by dynamic NMR spectroscopy
    • Kern D, Kern G, Scherer G, Fischer G, Drakenberg T. Kinetic analysis of cyclophilin-catalyzed prolyl cis/trans isomerization by dynamic NMR spectroscopy. Biochemistry 1995;34:13594-13602.
    • (1995) Biochemistry , vol.34 , pp. 13594-13602
    • Kern, D.1    Kern, G.2    Scherer, G.3    Fischer, G.4    Drakenberg, T.5
  • 63
    • 0035827163 scopus 로고    scopus 로고
    • Inclusion of quantum mechanical vibrational energy in reactive potentials of mean force
    • Garcia-Viloca M, Alhambra C, Truhlar DG, Gao J. Inclusion of quantum mechanical vibrational energy in reactive potentials of mean force. J Chem Phys 2001;114:9953-9958.
    • (2001) J Chem Phys , vol.114 , pp. 9953-9958
    • Garcia-Viloca, M.1    Alhambra, C.2    Truhlar, D.G.3    Gao, J.4
  • 65
    • 0142026621 scopus 로고    scopus 로고
    • Generalized transition state theory in terms of the potential of mean force
    • Schenter GK, Garrett BC, Truhlar DG. Generalized transition state theory in terms of the potential of mean force. J Chem Phys 2003;119:5828-5833.
    • (2003) J Chem Phys , vol.119 , pp. 5828-5833
    • Schenter, G.K.1    Garrett, B.C.2    Truhlar, D.G.3
  • 66
    • 0030666230 scopus 로고    scopus 로고
    • Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein
    • Vajdos FE, Yoo SH, Houseweart M, Sundquist WI, Hill CP. Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein. Protein Sci 1997;6:2297-2307.
    • (1997) Protein Sci , vol.6 , pp. 2297-2307
    • Vajdos, F.E.1    Yoo, S.H.2    Houseweart, M.3    Sundquist, W.I.4    Hill, C.P.5
  • 67
    • 0037178118 scopus 로고    scopus 로고
    • The mechanism of cis-trans isomerization of prolyl peptides by cyclophilin
    • Hur S, Bruice TC. The mechanism of cis-trans isomerization of prolyl peptides by cyclophilin. J Am Chem Soc 2002;124:7303-7313.
    • (2002) J Am Chem Soc , vol.124 , pp. 7303-7313
    • Hur, S.1    Bruice, T.C.2


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