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Volumn 100, Issue 4, 2011, Pages 1066-1075

Enantiospecificity of chloroperoxidase-catalyzed epoxidation: Biased molecular dynamics study of a cis-β-methylstyrene/chloroperoxidase-Compound I complex

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EID: 79951832315     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.12.3729     Document Type: Article
Times cited : (13)

References (56)
  • 1
    • 0014027412 scopus 로고
    • Chloroperoxidase. I. Isolation and properties of the crystalline glycoprotein
    • Morris, D. R., and L. P. Hager. 1966. Chloroperoxidase. I. Isolation and properties of the crystalline glycoprotein. J. Biol. Chem. 241:1763-1768.
    • (1966) J. Biol. Chem. , vol.241 , pp. 1763-1768
    • Morris, D.R.1    Hager, L.P.2
  • 2
    • 0014027368 scopus 로고
    • Chloroperoxidase. II. Utilization of halogen anions
    • Hager, L. P., D. R. Morris, H. Eberwein. 1966. Chloroperoxidase. II. Utilization of halogen anions. J. Biol. Chem. 241:1769-1777.
    • (1966) J. Biol. Chem. , vol.241 , pp. 1769-1777
    • Hager, L.P.1    Morris, D.R.2    Eberwein, H.3
  • 3
    • 0029786641 scopus 로고    scopus 로고
    • Quantitating direct chlorine transfer from enzyme to substrate in chloroperoxidase-catalyzed reactions
    • DOI 10.1074/jbc.271.36.21820
    • Libby, R. D., T. M. Beachy, and A. K. Phipps. 1996. Quantitating direct chlorine transfer from enzyme to substrate in chloroperoxidasecatalyzed reactions. J. Biol. Chem. 271:21820-21827. (Pubitemid 26303801)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.36 , pp. 21820-21827
    • Libby, R.D.1    Beachy, T.M.2    Phipps, A.K.3
  • 4
    • 0014802905 scopus 로고
    • Chloroperoxidase. VII. Classical peroxidatic, catalatic, and halogenating forms of the enzyme
    • Thomas, J. A., D. R. Morris, and L. P. Hager. 1970. Chloroperoxidase. VII. Classical peroxidatic, catalatic, and halogenating forms of the enzyme. J. Biol. Chem. 245:3129-3134.
    • (1970) J. Biol. Chem. , vol.245 , pp. 3129-3134
    • Thomas, J.A.1    Morris, D.R.2    Hager, L.P.3
  • 5
    • 0028361241 scopus 로고
    • The chloroperoxidase-catalyzed oxidation of phenols. Mechanism, selectivity, and characterization of enzyme-substrate complexes
    • DOI 10.1021/bi00187a001
    • Casella, L., S. Poli, A. Marchesini. 1994. The chloroperoxidasecatalyzed oxidation of phenols. Mechanism, selectivity, and characterization of enzyme-substrate complexes. Biochemistry. 33:6377-6386. (Pubitemid 24189346)
    • (1994) Biochemistry , vol.33 , Issue.21 , pp. 6377-6386
    • Casella, L.1    Poli, S.2    Gullotti, M.3    Selvaggini, C.4    Beringhelli, T.5    Marchesini, A.6
  • 6
    • 0023664820 scopus 로고
    • Structure-mechanism relationships in hemoproteins. Oxygenations catalyzed by chloroperoxidase and horseradish peroxidase
    • Ortiz de Montellano, P. R., Y. S. Choe, C. E. Catalano. 1987. Structure-mechanism relationships in hemoproteins. Oxygenations catalyzed by chloroperoxidase and horseradish peroxidase. J. Biol. Chem. 262:11641-11646.
    • (1987) J. Biol. Chem. , vol.262 , pp. 11641-11646
    • Ortiz De Montellano, P.R.1    Choe, Y.S.2    Catalano, C.E.3
  • 7
    • 0024294403 scopus 로고
    • Probing structure-function relations in hemecontaining oxygenases and peroxidases
    • Dawson, J. H. 1988. Probing structure-function relations in hemecontaining oxygenases and peroxidases. Science. 240:433-439.
    • (1988) Science , vol.240 , pp. 433-439
    • Dawson, J.H.1
  • 9
    • 36849034992 scopus 로고    scopus 로고
    • Caldariomyces fumago chloroperoxidase catalyzes the oxidative dehalogenation of chlorophenols by a mechanism involving two one-electron steps
    • DOI 10.1021/ja0746969
    • Osborne, R. L., M. K. Coggins, J. H. Dawson. 2007. Caldariomyces fumago chloroperoxidase catalyzes the oxidative dehalogenation of chlorophenols by a mechanism involving two one-electron steps. J. Am. Chem. Soc. 129:14838-14839. (Pubitemid 350230691)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.48 , pp. 14838-14839
    • Osborne, R.L.1    Coggins, M.K.2    Terner, J.3    Dawson, J.H.4
  • 10
    • 55549139465 scopus 로고    scopus 로고
    • Atypical kinetic behavior of chloroperoxidase-mediated oxidative halogenation of polycyclic aromatic hydrocarbons
    • Aburto, J., J. Correa-Basurto, and E. Torres. 2008. Atypical kinetic behavior of chloroperoxidase-mediated oxidative halogenation of polycyclic aromatic hydrocarbons. Arch. Biochem. Biophys. 480:33-40.
    • (2008) Arch. Biochem. Biophys. , vol.480 , pp. 33-40
    • Aburto, J.1    Correa-Basurto, J.2    Torres, E.3
  • 12
    • 40349098653 scopus 로고    scopus 로고
    • Chloroperoxidase, a janus enzyme
    • DOI 10.1021/bi7022656
    • Manoj, K. M., and L. P. Hager. 2008. Chloroperoxidase, a Janus enzyme. Biochemistry. 47:2997-3003. (Pubitemid 351337538)
    • (2008) Biochemistry , vol.47 , Issue.9 , pp. 2997-3003
    • Manoj, K.M.1    Hager, L.P.2
  • 13
    • 37449004862 scopus 로고    scopus 로고
    • Enhanced catalytic performance and stability of chloroperoxidase from Caldariomyces fumago in surfactant free ternary water-organic solvent systems
    • Tzialla, A. A., E. Kalogeris, H. Stamatis. 2008. Enhanced catalytic performance and stability of chloroperoxidase from Caldariomyces fumago in surfactant free ternary water-organic solvent systems. J. Mol. Catal., B Enzym. 51:24-35.
    • (2008) J. Mol. Catal., B. Enzym. , vol.51 , pp. 24-35
    • Tzialla, A.A.1    Kalogeris, E.2    Stamatis, H.3
  • 14
    • 85031247909 scopus 로고    scopus 로고
    • Dynamics and energetics associated with ligand photodissociation from CO bound chloroperoxidase
    • Horsa, S., L. Jiang, J. Miksovska. 2009. Dynamics and energetics associated with ligand photodissociation from CO bound chloroperoxidase. Biophys. J. 96 (Supplement 1): 437):437a.
    • (2009) Biophys. J. , vol.96 , Issue.1 SUPPL.
    • Horsa, S.1    Jiang, L.2    Miksovska, J.3
  • 15
    • 85031258814 scopus 로고    scopus 로고
    • Structural dynamics in chloroperoxidase: A photoacoustic study
    • Horsa, S., X. Wang, and J. Miksovska. 2010. Structural dynamics in chloroperoxidase: a photoacoustic study. Biophys. J. 98 (Supplement 1): 643):643a.
    • (2010) Biophys. J. , vol.98 , Issue.1 SUPPL.
    • Horsa, S.1    Wang, X.2    Miksovska, J.3
  • 16
    • 0034685476 scopus 로고    scopus 로고
    • Probing the role of protein environment in compound I formation of chloroperoxidase (CPO)
    • DOI 10.1021/ja993000b
    • Filizola, M., and G. H. Loew. 2000. Probing the role of protein environment in compound I formation of chloroperoxidase (CPO). J. Am. Chem. Soc. 122:3599-3605. (Pubitemid 30233429)
    • (2000) Journal of the American Chemical Society , vol.122 , Issue.15 , pp. 3599-3605
    • Filizola, M.1    Loew, G.H.2
  • 17
    • 49649112644 scopus 로고    scopus 로고
    • Quantum mechanical/molecular mechanical study on the mechanisms of compound I formation in the catalytic cycle of chloroperoxidase: An overview on heme enzymes
    • Chen, H., H. Hirao, S. Shaik. 2008. Quantum mechanical/molecular mechanical study on the mechanisms of compound I formation in the catalytic cycle of chloroperoxidase: an overview on heme enzymes. J. Phys. Chem. B. 112:9490-9500.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 9490-9500
    • Chen, H.1    Hirao, H.2    Shaik, S.3
  • 18
    • 70350776835 scopus 로고    scopus 로고
    • Effects of substrate, protein environment, and proximal ligand mutation on compound I and compound 0 of chloroperoxidase
    • Lai, W. Z., H. Chen, S. Shaik. 2009. Effects of substrate, protein environment, and proximal ligand mutation on compound I and compound 0 of chloroperoxidase. J. Phys. Chem. A. 113:11763-11771.
    • (2009) J. Phys. Chem. A , vol.113 , pp. 11763-11771
    • Lai, W.Z.1    Chen, H.2    Shaik, S.3
  • 19
    • 66549089347 scopus 로고    scopus 로고
    • What kinds of ferryl species exist for compound II of chloroperoxidase? A dialog of theory with experiment
    • Lai, W. Z., H. Chen, and S. Shaik. 2009. What kinds of ferryl species exist for compound II of chloroperoxidase? A dialog of theory with experiment. J. Phys. Chem. B. 113:7912-7917.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 7912-7917
    • Lai, W.Z.1    Chen, H.2    Shaik, S.3
  • 20
    • 0025223821 scopus 로고
    • Enantioselective oxidations of sulfides catalyzed by chloroperoxidase
    • Colonna, S., N. Gaggero, P. Pasta. 1990. Enantioselective oxidations of sulfides catalyzed by chloroperoxidase. Biochemistry. 29:10465-10468.
    • (1990) Biochemistry , vol.29 , pp. 10465-10468
    • Colonna, S.1    Gaggero, N.2    Pasta, P.3
  • 21
    • 9344259269 scopus 로고
    • Highly enantioselective epoxidation of disubstituted alkenes with hydrogen peroxide catalyzed by chloroperoxidase
    • Allain, E. J., L. P. Hager, E. N. Jacobsen. 1993. Highly enantioselective epoxidation of disubstituted alkenes with hydrogen peroxide catalyzed by chloroperoxidase. J. Am. Chem. Soc. 115:4415-4416.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 4415-4416
    • Allain, E.J.1    Hager, L.P.2    Jacobsen, E.N.3
  • 22
    • 0033518595 scopus 로고    scopus 로고
    • Highly enantioselective propargylic hydroxylations catalyzed by chloroperoxidase [9]
    • DOI 10.1021/ja983612g
    • Hu, S., and L. P. Hager. 1999. Highly enantioselective propargylic hydroxylations catalyzed by chloroperoxidase. J. Am. Chem. Soc. 121:872-873. (Pubitemid 29077313)
    • (1999) Journal of the American Chemical Society , vol.121 , Issue.4 , pp. 872-873
    • Hu, S.1    Hager, L.P.2
  • 23
    • 0029646104 scopus 로고
    • The crystal structure of chloroperoxidase: A heme peroxidase-cytochrome P450 functional hybrid
    • DOI 10.1016/S0969-2126(01)00274-X
    • Sundaramoorthy, M., J. Terner, and T. L. Poulos. 1995. The crystal structure of chloroperoxidase: a heme peroxidase-cytochrome P450 functional hybrid. Structure. 3:1367-1377. (Pubitemid 3012264)
    • (1995) Structure , vol.3 , Issue.12 , pp. 1367-1377
    • Sundaramoorthy, M.1    Terner, J.2    Poulos, T.L.3
  • 24
    • 0037515622 scopus 로고    scopus 로고
    • Examining the role of glutamic acid 183 in chloroperoxidase catalysis
    • DOI 10.1074/jbc.M210906200
    • Yi, X., A. Conesa, L. P. Hager. 2003. Examining the role of glutamic acid 183 in chloroperoxidase catalysis. J. Biol. Chem. 278:13855-13859. (Pubitemid 36799924)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.16 , pp. 13855-13859
    • Yi, X.1    Conesa, A.2    Punt, P.J.3    Hager, L.P.4
  • 25
    • 0037424350 scopus 로고    scopus 로고
    • Two-dimensional NMR study of the heme active site structure of chloroperoxidase
    • DOI 10.1074/jbc.M209462200
    • Wang, X., H. Tachikawa, L. P. Hager. 2003. Two-dimensional NMR study of the heme active site structure of chloroperoxidase. J. Biol. Chem. 278:7765-7774. (Pubitemid 36800509)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.10 , pp. 7765-7774
    • Wang, X.1    Tachikawa, H.2    Yi, X.3    Manoj, K.M.4    Hager, L.P.5
  • 26
    • 33747732175 scopus 로고    scopus 로고
    • Crystal structures of chloroperoxidase with its bound substrates and complexed with formate, acetate, and nitrate
    • DOI 10.1074/jbc.M603166200
    • Kühnel, K., W. Blankenfeldt, I. Schlichting. 2006. Crystal structures of chloroperoxidase with its bound substrates and complexed with formate, acetate, and nitrate. J. Biol. Chem. 281:23990-23998. (Pubitemid 44274173)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.33 , pp. 23990-23998
    • Kuhnel, K.1    Blankenfeldt, W.2    Terner, J.3    Schlichting, I.4
  • 27
    • 0032170496 scopus 로고    scopus 로고
    • Stereochemistry of the chloroperoxidase active site: Crystallographic and molecular-modeling studies
    • Sundaramoorthy, M., J. Terner, and T. L. Poulos. 1998. Stereochemistry of the chloroperoxidase active site: crystallographic and molecular-modeling studies. Chem. Biol. 5:461-473. (Pubitemid 28436725)
    • (1998) Chemistry and Biology , vol.5 , Issue.9 , pp. 461-473
    • Sundaramoorthy, M.1    Terner, J.2    Poulos, T.L.3
  • 28
    • 0033605393 scopus 로고    scopus 로고
    • Asymmetric epoxidation of functionalized cis-olefins catalyzed by chloroperoxidase
    • DOI 10.1016/S0040-4039(99)00056-8, PII S0040403999000568
    • Hu, S., and L. P. Hager. 1999. Asymmetric epoxidation of functionalized cis-olefins catalyzed by chloroperoxidase. Tetrahedron Lett. 40:1641-1644. (Pubitemid 29087263)
    • (1999) Tetrahedron Letters , vol.40 , Issue.9 , pp. 1641-1644
    • Hu, S.1    Hager, L.P.2
  • 30
    • 0034692380 scopus 로고    scopus 로고
    • A model "rebound" mechanism of hydroxylation by cytochrome P450: Stepwise and effectively concerted pathways, and their reactivity patterns
    • Ogliaro, F., N. Harris, S. Shaik. 2000. A model "rebound" mechanism of hydroxylation by cytochrome P450: stepwise and effectively concerted pathways, and their reactivity patterns. J. Am. Chem. Soc. 122:8977-8989.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 8977-8989
    • Ogliaro, F.1    Harris, N.2    Shaik, S.3
  • 31
    • 0036802621 scopus 로고    scopus 로고
    • Two-state reactivity mechanisms of hydroxylation and epoxidation by cytochrome P-450 revealed by theory
    • DOI 10.1016/S1367-5931(02)00363-0
    • Shaik, S., S. P. de Visser, D. Schröder. 2002. Two-state reactivity mechanisms of hydroxylation and epoxidation by cytochrome P-450 revealed by theory. Curr. Opin. Chem. Biol. 6:556-567. (Pubitemid 35284185)
    • (2002) Current Opinion in Chemical Biology , vol.6 , Issue.5 , pp. 556-567
    • Shaik, S.1    De Visser, S.P.2    Ogliaro, F.3    Schwarz, H.4    Schroder, D.5
  • 32
  • 33
    • 0000370697 scopus 로고
    • Calculated and experimental absolute stereochemistry of the styrene and β-methylstyrene epoxides formed by cytochrome P 450cam
    • Fruetel, J. A., J. R. Collins, P. R. Ortiz de Montellano. 1992. Calculated and experimental absolute stereochemistry of the styrene and β-methylstyrene epoxides formed by cytochrome P 450cam. J. Am. Chem. Soc. 114:6987-6993.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6987-6993
    • Fruetel, J.A.1    Collins, J.R.2    Ortiz De Montellano, P.R.3
  • 34
    • 64049102289 scopus 로고    scopus 로고
    • Binding of small-molecule ligands to proteins: "What you see" is not always "what you get"
    • Mobley, D. L., and K. A. Dill. 2009. Binding of small-molecule ligands to proteins: "what you see" is not always "what you get". Structure. 17:489-498.
    • (2009) Structure , vol.17 , pp. 489-498
    • Mobley, D.L.1    Dill, K.A.2
  • 35
    • 0342929614 scopus 로고
    • Nonphysical sampling distributions in Monte Carlo free-energy estimation: Umbrella sampling
    • Torrie, G. M., and J. P. Valleau. 1977. Nonphysical sampling distributions in Monte Carlo free-energy estimation: umbrella sampling. J. Comput. Phys. 23:187-199.
    • (1977) J. Comput. Phys. , vol.23 , pp. 187-199
    • Torrie, G.M.1    Valleau, J.P.2
  • 36
    • 33646987405 scopus 로고
    • Optimized Monte Carlo data analysis
    • Ferrenberg, A. M., and R. H. Swendsen. 1989. Optimized Monte Carlo data analysis. Phys. Rev. Lett. 63:1195-1198.
    • (1989) Phys. Rev. Lett. , vol.63 , pp. 1195-1198
    • Ferrenberg, A.M.1    Swendsen, R.H.2
  • 37
    • 84986519238 scopus 로고
    • The weighted histogram analysis method for free-energy calculations on biomolecules. I. The Method
    • Shankar, K., M. R. John, A. K. Peter. 1992. The weighted histogram analysis method for free-energy calculations on biomolecules. I. The method. J. Comput. Chem. 13:1011-1021.
    • (1992) J. Comput. Chem. , vol.13 , pp. 1011-1021
    • Shankar, K.1    John, M.R.2    Peter, A.K.3
  • 38
    • 0000087970 scopus 로고
    • An adaptive umbrella sampling procedure in conformational analysis using molecular dynamics and its application to glycol
    • Hooft, R. W. W., B. P. van Eijck, and J. Kroon. 1992. An adaptive umbrella sampling procedure in conformational analysis using molecular dynamics and its application to glycol. J. Chem. Phys. 97:6690-6694.
    • (1992) J. Chem. Phys. , vol.97 , pp. 6690-6694
    • Hooft, R.W.W.1    Van Eijck, B.P.2    Kroon, J.3
  • 39
    • 6644221271 scopus 로고    scopus 로고
    • Efficient, multiple-range random walk algorithm to calculate the density of states
    • DOI 10.1103/PhysRevLett.86.2050
    • Wang, F., and D. P. Landau. 2001. Efficient, multiple-range random walk algorithm to calculate the density of states. Phys. Rev. Lett. 86:2050-2053. (Pubitemid 32254758)
    • (2001) Physical Review Letters , vol.86 , Issue.10 , pp. 2050-2053
    • Wang, F.1    Landau, D.P.2
  • 40
    • 60749120298 scopus 로고    scopus 로고
    • Thermodynamics of a conformational change using a random walk in energy-reaction coordinate space: Application to methane dimer hydrophobic interactions
    • Morozov, A. N., and S. H. Lin. 2009. Thermodynamics of a conformational change using a random walk in energy-reaction coordinate space: application to methane dimer hydrophobic interactions. J. Chem. Phys. 130:074903-074909.
    • (2009) J. Chem. Phys. , vol.130 , pp. 074903-074909
    • Morozov, A.N.1    Lin, S.H.2
  • 43
    • 0001102309 scopus 로고    scopus 로고
    • The alanine dipeptide free energy surface in solution
    • Smith, P. E. 1999. The alanine dipeptide free energy surface in solution. J. Chem. Phys. 111:5568-5579.
    • (1999) J. Chem. Phys. , vol.111 , pp. 5568-5579
    • Smith, P.E.1
  • 44
    • 33748563197 scopus 로고    scopus 로고
    • Determination of conformational free energies of peptides by multidimensional adaptive umbrella sampling
    • Wang, J., Y. Gu, and H. Liu. 2006. Determination of conformational free energies of peptides by multidimensional adaptive umbrella sampling. J. Chem. Phys. 125:094907-094909.
    • (2006) J. Chem. Phys. , vol.125 , pp. 094907-094909
    • Wang, J.1    Gu, Y.2    Liu, H.3
  • 47
    • 3142714765 scopus 로고    scopus 로고
    • Extending the treatment of backbone energetics in protein force fields: Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations
    • Mackerell, Jr., A. D., M. Feig, and C. L. Brooks, 3rd. 2004. Extending the treatment of backbone energetics in protein force fields: limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations. J. Comput. Chem. 25:1400-1415.
    • (2004) J. Comput. Chem. , vol.25 , pp. 1400-1415
    • Mackerell Jr., A.D.1    Feig, M.2    Brooks III, C.L.3
  • 48
    • 0037464481 scopus 로고    scopus 로고
    • Construction and assessment of models of CYP2E1: Predictions of metabolism from docking, molecular dynamics, and density functional theoretical calculations
    • DOI 10.1021/jm020538a
    • Park, J. Y., and D. Harris. 2003. Construction and assessment of models of CYP2E1: predictions of metabolism from docking, molecular dynamics, and density functional theoretical calculations. J. Med. Chem. 46:1645-1660. (Pubitemid 36444218)
    • (2003) Journal of Medicinal Chemistry , vol.46 , Issue.9 , pp. 1645-1660
    • Park, J.-Y.1    Harris, D.2
  • 49
    • 76249087938 scopus 로고    scopus 로고
    • CHARMM general force field: A force field for drug-like molecules compatible with the CHARMM all-atom additive biological force fields
    • Vanommeslaeghe, K., E. Hatcher, A. D. Mackerell, Jr. 2010. CHARMM general force field: a force field for drug-like molecules compatible with the CHARMM all-atom additive biological force fields. J. Comput. Chem. 31:671-690.
    • (2010) J. Comput. Chem. , vol.31 , pp. 671-690
    • Vanommeslaeghe, K.1    Hatcher, E.2    Mackerell Jr., A.D.3
  • 51
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert, J.-P., G. Ciccotti, and H. J. C. Berendsen. 1977. Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J. Comput. Phys. 23:327-341.
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.-P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 52
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distributions
    • Hoover, W. G. 1985. Canonical dynamics: equilibrium phase-space distributions. Phys. Rev. A. 31:1695-1697.
    • (1985) Phys. Rev. A , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 54
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • Jorgensen, W. L., J. Chandrasekhar, M. L. Klein. 1983. Comparison of simple potential functions for simulating liquid water. J. Chem. Phys. 79:926-935.
    • (1983) J. Chem. Phys. , vol.79 , pp. 926-935
    • Jorgensen, W.L.1    Chandrasekhar, J.2    Klein, M.L.3
  • 55
    • 0020160864 scopus 로고
    • Dynamical theory of activated processes in globular proteins
    • Northrup, S. H., M. R. Pear, M. Karplus. 1982. Dynamical theory of activated processes in globular proteins. Proc. Natl. Acad. Sci. USA. 79:4035-4039.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 4035-4039
    • Northrup, S.H.1    Pear, M.R.2    Karplus, M.3
  • 56
    • 0000071835 scopus 로고    scopus 로고
    • Motion and conformation of side chains in peptides. A comparison of 2D umbrella-sampling molecular dynamics and NMR Results
    • Beutler, T. C., T. Bremi, W. F. van Gunsteren. 1996. Motion and conformation of side chains in peptides. A comparison of 2D umbrella-sampling molecular dynamics and NMR results. J. Phys. Chem. 100:2637-2645. (Pubitemid 126793216)
    • (1996) Journal of Physical Chemistry , vol.100 , Issue.7 , pp. 2637-2645
    • Beutler, T.C.1    Bremi, T.2    Ernst, R.R.3    Van Gunsteren, W.F.4


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