메뉴 건너뛰기




Volumn 32, Issue 2, 1998, Pages 136-158

Protein folding mechanisms and the multidimensional folding funnel

Author keywords

Folding funnels; Landscape theory; Lattice models; Monte Carlo simulations

Indexed keywords

ARTICLE; ENERGY; HYDROPHOBICITY; KINETICS; MODEL; PRIORITY JOURNAL; PROTEIN FOLDING; SYSTEM ANALYSIS; THERMODYNAMICS;

EID: 0032147243     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19980801)32:2<136::AID-PROT2>3.0.CO;2-J     Document Type: Article
Times cited : (189)

References (78)
  • 1
    • 0023449962 scopus 로고
    • Spin glasses and the statistical mechanics of protein folding
    • Bryngelson, J.D., Wolynes, P.G. Spin glasses and the statistical mechanics of protein folding. Proc. Natl. Acad. Sci. U.S.A. 84:7524-7528, 1987.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 7524-7528
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 2
    • 0024733407 scopus 로고
    • Intermediates and barrier crossing in a random energy model (with applications to protein folding)
    • Bryngelson, J.D., Wolynes, P.G. Intermediates and barrier crossing in a random energy model (with applications to protein folding). J. Phys. Chem. 93:6902-6915, 1989.
    • (1989) J. Phys. Chem. , vol.93 , pp. 6902-6915
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 3
    • 0025148817 scopus 로고
    • A simple statistical field theory of heteropolymer collapse with application to protein folding
    • Bryngelson, J.D., Wolynes, P.G. A simple statistical field theory of heteropolymer collapse with application to protein folding. Biopolymers 30:177-188, 1990.
    • (1990) Biopolymers , vol.30 , pp. 177-188
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 4
    • 0026723063 scopus 로고
    • Protein folding funnels: Kinetic pathways through compact conformational space
    • Leopold, P.E., Montal, M., Onuchic, J.N. Protein folding funnels: Kinetic pathways through compact conformational space. Proc. Natl. Acad. Sci. U.S.A. 89:8721-8725, 1992.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 8721-8725
    • Leopold, P.E.1    Montal, M.2    Onuchic, J.N.3
  • 5
    • 0000868733 scopus 로고
    • The protein folding problem
    • Chan, H.S., Dill, K.A. The protein folding problem. Phys. Today 46:24-32, 1993.
    • (1993) Phys. Today , vol.46 , pp. 24-32
    • Chan, H.S.1    Dill, K.A.2
  • 6
    • 36449008575 scopus 로고
    • Energy landscapes and the collapse dynamics of homopolymers
    • Chan, H.S., Dill, K.A. Energy landscapes and the collapse dynamics of homopolymers. J. Chem. Phys. 99:2116-2127, 1993.
    • (1993) J. Chem. Phys. , vol.99 , pp. 2116-2127
    • Chan, H.S.1    Dill, K.A.2
  • 7
    • 0027318781 scopus 로고
    • Kinetics and thermodynamics of folding in model proteins
    • Camacho, C.J., Thirumalai, D. Kinetics and thermodynamics of folding in model proteins. Proc. Natl. Acad. Sci. U.S.A. 90:6369-6372, 1993.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 6369-6372
    • Camacho, C.J.1    Thirumalai, D.2
  • 8
    • 36448999595 scopus 로고
    • Free energy landscape for protein folding kinetics: Intermediates, traps and multiple pathways in theory and lattice model simulations
    • Abkevich, V.I., Gutin, A.M., Shakhnovich, E.I. Free energy landscape for protein folding kinetics: Intermediates, traps and multiple pathways in theory and lattice model simulations. J. Chem. Phys. 101:6052-6062, 1994.
    • (1994) J. Chem. Phys. , vol.101 , pp. 6052-6062
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 9
    • 0028947257 scopus 로고
    • Funnels, pathways and the energy landscape of protein folding: A synthesis
    • Bryngelson, J.D., Onuchic, J.N., Socci, N.D., Wolynes, RG. Funnels, pathways and the energy landscape of protein folding: A synthesis. Proteins 21:167-195, 1995.
    • (1995) Proteins , vol.21 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, R.G.4
  • 12
    • 0029151245 scopus 로고
    • First-principles calculation of the folding free energy of a three-helix bundle protein
    • Boczko, E.M., Brooks, C.L. First-principles calculation of the folding free energy of a three-helix bundle protein. Science 269:393-396, 1995.
    • (1995) Science , vol.269 , pp. 393-396
    • Boczko, E.M.1    Brooks, C.L.2
  • 13
    • 0000710672 scopus 로고    scopus 로고
    • Diffusive dynamics of the reaction coordinate for protein folding funnels
    • Socci, N.D., Onuchic, J.N., Wolynes, P.G. Diffusive dynamics of the reaction coordinate for protein folding funnels. J. Chem. Phys. 104:5860-5868, 1996.
    • (1996) J. Chem. Phys. , vol.104 , pp. 5860-5868
    • Socci, N.D.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 15
    • 0030155292 scopus 로고    scopus 로고
    • Fast-folding experiments and the topography of protein folding energy landscapes
    • Wolynes, P.G., Schulten, Z.L., Onuchic, J. Fast-folding experiments and the topography of protein folding energy landscapes. Chem Biol 3:425-432, 1996.
    • (1996) Chem Biol , vol.3 , pp. 425-432
    • Wolynes, P.G.1    Schulten, Z.L.2    Onuchic, J.3
  • 16
    • 0030334626 scopus 로고    scopus 로고
    • Universality and diversity of the protein folding scenarios: A comprehensive analysis with the aid of a lattice model
    • Mirny, L.A., Abkevich, V., Shakhnovich, E.I. Universality and diversity of the protein folding scenarios: A comprehensive analysis with the aid of a lattice model. Folding Design 1:103-116, 1996.
    • (1996) Folding Design , vol.1 , pp. 103-116
    • Mirny, L.A.1    Abkevich, V.2    Shakhnovich, E.I.3
  • 17
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill, K.A., Chan, H.S. From Levinthal to pathways to funnels. Nature Struct. Biol. 4:10-19, 1997.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 18
    • 0027219504 scopus 로고
    • Protein unfolding pathways explored through molecular dynamics simulations
    • Daggett, V., Levitt, M. Protein unfolding pathways explored through molecular dynamics simulations. J. Mol. Biol. 232:600-619, 1993.
    • (1993) J. Mol. Biol. , vol.232 , pp. 600-619
    • Daggett, V.1    Levitt, M.2
  • 19
    • 0028203492 scopus 로고
    • Monte Carlo simulations of protein folding. I. Lattice. model and interaction scheme
    • Kolinski, A., Skolnick, J. Monte Carlo simulations of protein folding. I. Lattice. model and interaction scheme. Proteins 18:338-352, 1994.
    • (1994) Proteins , vol.18 , pp. 338-352
    • Kolinski, A.1    Skolnick, J.2
  • 20
    • 0028326042 scopus 로고
    • Monte Carlo simulations of protein folding. II. Application to protein A, ROP, and crambin
    • Kolinski, A., Skolnick, J. Monte Carlo simulations of protein folding. II. Application to protein A, ROP, and crambin. Proteins 18:353-366, 1994.
    • (1994) Proteins , vol.18 , pp. 353-366
    • Kolinski, A.1    Skolnick, J.2
  • 21
    • 0028270634 scopus 로고
    • Kinetics of protein folding: A lattice model study of the requirements for folding to the native state
    • Šali, A., Shakhnovich, E., Karplus, M. Kinetics of protein folding: A lattice model study of the requirements for folding to the native state. J. Mol. Biol. 235:1614-1636, 1994.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1614-1636
    • Šali, A.1    Shakhnovich, E.2    Karplus, M.3
  • 22
    • 0000515198 scopus 로고
    • Monte Carlo simulation of a first-order transition for protein folding
    • Hao, M.-H., Scheraga, H.A. Monte Carlo simulation of a first-order transition for protein folding. J. Phys. Chem. 98:4940-4948, 1994.
    • (1994) J. Phys. Chem. , vol.98 , pp. 4940-4948
    • Hao, M.-H.1    Scheraga, H.A.2
  • 23
    • 0003166498 scopus 로고    scopus 로고
    • Protein folding in the landscape perspective
    • Chan, H.S., Dill, K.A. Protein folding in the landscape perspective. Proteins 30:2-33, 1998.
    • (1998) Proteins , vol.30 , pp. 2-33
    • Chan, H.S.1    Dill, K.A.2
  • 24
    • 0031555012 scopus 로고    scopus 로고
    • The foldability landscape of model proteins
    • Govindarajan, S., Goldstein, R.A. The foldability landscape of model proteins. Biopolymers 42:427-438, 1997.
    • (1997) Biopolymers , vol.42 , pp. 427-438
    • Govindarajan, S.1    Goldstein, R.A.2
  • 25
    • 0030057477 scopus 로고
    • Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues
    • Khorasanizadeh, S., Peters, I.D., Roder, H. Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues. Nature Struct. Biol. 2:193-205, 1995.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 193-205
    • Khorasanizadeh, S.1    Peters, I.D.2    Roder, H.3
  • 26
    • 0029010695 scopus 로고
    • Kinetics of protein folding: Nucleation mechanism, time scales, and pathways
    • Guo, Z.Y., Thirumalai, D. Kinetics of protein folding: Nucleation mechanism, time scales, and pathways. Biopolymers 36:83-102, 1995.
    • (1995) Biopolymers , vol.36 , pp. 83-102
    • Guo, Z.Y.1    Thirumalai, D.2
  • 27
    • 0028835443 scopus 로고
    • Nucleation mechanism for protein folding and theoretical predictions for hydrogen-exchange labeling experiments
    • Thirumalai, D., Guo, Z.Y. Nucleation mechanism for protein folding and theoretical predictions for hydrogen-exchange labeling experiments. Biopolymers 35:137-140, 1995.
    • (1995) Biopolymers , vol.35 , pp. 137-140
    • Thirumalai, D.1    Guo, Z.Y.2
  • 28
    • 0007463680 scopus 로고    scopus 로고
    • Statistical mechanics of a correlated energy landscape model for protein folding funnels
    • Plotkin, S.S., Wang, J., Wolynes, P.G. Statistical mechanics of a correlated energy landscape model for protein folding funnels. J. Chem. Phys. 106:2932, 1997.
    • (1997) J. Chem. Phys. , vol.106 , pp. 2932
    • Plotkin, S.S.1    Wang, J.2    Wolynes, P.G.3
  • 29
    • 0001669870 scopus 로고
    • Kinetic and thermodynamic analysis of proteinlike heteropolymers: Monte Carlo histogram technique
    • Socci, N.D., Onuchic, J.N. Kinetic and thermodynamic analysis of proteinlike heteropolymers: Monte Carlo histogram technique. J. Chem. Phys. 103:4732-4744, 1995.
    • (1995) J. Chem. Phys. , vol.103 , pp. 4732-4744
    • Socci, N.D.1    Onuchic, J.N.2
  • 30
    • 0007725036 scopus 로고
    • Folding kinetics of proteinlike heteropolymers
    • Socci, N.D., Onuchic, J.N. Folding kinetics of proteinlike heteropolymers. J. Chem. Phys. 101:1519-1528, 1994.
    • (1994) J. Chem. Phys. , vol.101 , pp. 1519-1528
    • Socci, N.D.1    Onuchic, J.N.2
  • 32
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill, K.A. Dominant forces in protein folding. Biochemistry 29:7133-7155, 1990.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 34
    • 0029858841 scopus 로고    scopus 로고
    • Observation of distinct nanosecond and microsecond protein folding events
    • Ballew, R.M., Sabelko, J., Gruebele, M. Observation of distinct nanosecond and microsecond protein folding events. Nature Struct. Biol. 3:923-926, 1996.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 923-926
    • Ballew, R.M.1    Sabelko, J.2    Gruebele, M.3
  • 38
    • 0030967896 scopus 로고    scopus 로고
    • Exploring the folding free energy surface of a three helix bundle protein
    • Guo, Z., Brooks, C.L., Boczko, E.M. Exploring the folding free energy surface of a three helix bundle protein. Proc. Natl. Acad. Sci. U.S.A. 94:10161-10166, 1997.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 10161-10166
    • Guo, Z.1    Brooks, C.L.2    Boczko, E.M.3
  • 39
    • 0002689652 scopus 로고    scopus 로고
    • Thermodynamics of protein folding: A statistical mechanical study of a small all β protein
    • submitted
    • Guo, Z., Brooks, C.L. Thermodynamics of protein folding: A statistical mechanical study of a small all β protein. Biopolymers, submitted, 1997.
    • (1997) Biopolymers
    • Guo, Z.1    Brooks, C.L.2
  • 40
    • 0001143109 scopus 로고
    • Helix-coil, liquid crystal and spin glass transitions of a collapsed heteropolymer
    • Luthey-Schulten, Z., Ramirez, B.E., Wolynes, P.G. Helix-coil, liquid crystal and spin glass transitions of a collapsed heteropolymer. J. Phys. Chem. 99:2177-2185, 1995.
    • (1995) J. Phys. Chem. , vol.99 , pp. 2177-2185
    • Luthey-Schulten, Z.1    Ramirez, B.E.2    Wolynes, P.G.3
  • 41
    • 0030347890 scopus 로고    scopus 로고
    • All-or-none solvent-induced transitions between native, molten globule and unfolded states in globular proteins
    • Uversky, V.N., Ptitsyn, O.B. All-or-none solvent-induced transitions between native, molten globule and unfolded states in globular proteins. Folding Design 1:117-122, 1996.
    • (1996) Folding Design , vol.1 , pp. 117-122
    • Uversky, V.N.1    Ptitsyn, O.B.2
  • 42
    • 0001209011 scopus 로고    scopus 로고
    • Statistics of kinetic pathways on biased rough energy landscapes with applications to protein folding
    • Wang, J., Onuchic, J., Wolynes, P. Statistics of kinetic pathways on biased rough energy landscapes with applications to protein folding. Phys. Rev. Lett. 76:4861-1864, 1996.
    • (1996) Phys. Rev. Lett. , vol.76 , pp. 4861-11864
    • Wang, J.1    Onuchic, J.2    Wolynes, P.3
  • 43
    • 0000472973 scopus 로고    scopus 로고
    • Structure and dynamics of solvent landscapes in charge-transfer reactions
    • Leite, V.B.P., Onuchic, J.N. Structure and dynamics of solvent landscapes in charge-transfer reactions. J. Phys. Chem. 100:7680-7690, 1996.
    • (1996) J. Phys. Chem. , vol.100 , pp. 7680-7690
    • Leite, V.B.P.1    Onuchic, J.N.2
  • 45
    • 0026606219 scopus 로고
    • Effects of temperature on protein structure and dynamics: X-ray crystallographic studies of the protein ribonuclease-A at nine different temperatures from 98 to 320 K
    • Tilton, R., Dewan, J., Petsko, G. Effects of temperature on protein structure and dynamics: X-ray crystallographic studies of the protein ribonuclease-A at nine different temperatures from 98 to 320 K. Biochemistry 31:2469-2481, 1992.
    • (1992) Biochemistry , vol.31 , pp. 2469-2481
    • Tilton, R.1    Dewan, J.2    Petsko, G.3
  • 46
    • 0026636807 scopus 로고
    • The role of solvent viscosity in the dynamics of protein conformational changes
    • Ansari, A., Jones, C.M., Henry, E.R., Hofrichter, J., Eaton, W.A. The role of solvent viscosity in the dynamics of protein conformational changes. Science 256:1796-1798, 1992.
    • (1992) Science , vol.256 , pp. 1796-1798
    • Ansari, A.1    Jones, C.M.2    Henry, E.R.3    Hofrichter, J.4    Eaton, W.A.5
  • 47
    • 0009071257 scopus 로고
    • Formation of glasses from liquids and biopoly-mers
    • Angell, C.A. Formation of glasses from liquids and biopoly-mers. Science 267:1924-1935, 1995.
    • (1995) Science , vol.267 , pp. 1924-1935
    • Angell, C.A.1
  • 48
    • 21144471933 scopus 로고
    • Heat capacity of hydrated and dehydrated globular proteins
    • Sochava, I.V., Smirnova, O.I. Heat capacity of hydrated and dehydrated globular proteins. Food Hydrocolloids 6:513-524, 1993.
    • (1993) Food Hydrocolloids , vol.6 , pp. 513-524
    • Sochava, I.V.1    Smirnova, O.I.2
  • 50
    • 36449000646 scopus 로고
    • Transition states and folding dynamics of proteins and heteropolymers
    • Chan, H.S., Dill, K.A. Transition states and folding dynamics of proteins and heteropolymers. J. Chem. Phys. 100: 9238-9257, 1994.
    • (1994) J. Chem. Phys. , vol.100 , pp. 9238-9257
    • Chan, H.S.1    Dill, K.A.2
  • 51
    • 0030165480 scopus 로고    scopus 로고
    • Correlated energy landscape model for finite, random heteropolymers
    • Plotkin, S.S., Wang, J., Wolynes, P.G. Correlated energy landscape model for finite, random heteropolymers. Phys. Rev. E 53:6271-6296, 1996.
    • (1996) Phys. Rev. E , vol.53 , pp. 6271-6296
    • Plotkin, S.S.1    Wang, J.2    Wolynes, P.G.3
  • 52
    • 0001364489 scopus 로고    scopus 로고
    • Statics, metastable states and barriers in protein folding: A replica variational approach
    • Takada, S., Wolynes, P.G. Statics, metastable states and barriers in protein folding: A replica variational approach. Phys. Rev. E 55:4562, 1997.
    • (1997) Phys. Rev. E , vol.55 , pp. 4562
    • Takada, S.1    Wolynes, P.G.2
  • 53
    • 0031098769 scopus 로고    scopus 로고
    • Configurational diffusion on a locally connected correlated energy landscape: Application to finite random heteropolymers
    • France
    • Plotkin, S.S., Wang, J., Wolynes, P.G. Configurational diffusion on a locally connected correlated energy landscape: Application to finite random heteropolymers. J. Phys. I (France) 7:395, 1997.
    • (1997) J. Phys. I , vol.7 , pp. 395
    • Plotkin, S.S.1    Wang, J.2    Wolynes, P.G.3
  • 54
    • 0030283470 scopus 로고    scopus 로고
    • Dynamics of heteropolymers in dilute solution: Effective equation of motion and relaxation spectrum
    • Roan, J., Shakhnovich, E. Dynamics of heteropolymers in dilute solution: Effective equation of motion and relaxation spectrum. Phys. Rev. E 5:5340-5357, 1996.
    • (1996) Phys. Rev. E , vol.5 , pp. 5340-5357
    • Roan, J.1    Shakhnovich, E.2
  • 55
    • 0000091342 scopus 로고    scopus 로고
    • Dynamics of random hydrophobic-hydrophilic copolymers
    • Thirumalai, D., Ashwin, V., Bhattacharjee, J.K. Dynamics of random hydrophobic-hydrophilic copolymers. Phys. Rev. Lett, 77:5385-5388, 1996.
    • (1996) Phys. Rev. Lett , vol.77 , pp. 5385-5388
    • Thirumalai, D.1    Ashwin, V.2    Bhattacharjee, J.K.3
  • 56
    • 4243875619 scopus 로고    scopus 로고
    • Kinetics of a gaussian random copolymer as a prototype for protein folding
    • Timoshenko, E.G., Kuznetsov, Y.A., Dawson, K.A. Kinetics of a gaussian random copolymer as a prototype for protein folding. Phys. Rev. E 54:4071-4086, 1996.
    • (1996) Phys. Rev. E , vol.54 , pp. 4071-4086
    • Timoshenko, E.G.1    Kuznetsov, Y.A.2    Dawson, K.A.3
  • 57
    • 0030909596 scopus 로고    scopus 로고
    • An elementary mode coupling theory of random heteropolymer dynamics
    • Takada, S., Portman, J.J., Wolynes, P.G. An elementary mode coupling theory of random heteropolymer dynamics. Proc. Natl. Acad. Sci. U.S.A. 94:2318-2321, 1997.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 2318-2321
    • Takada, S.1    Portman, J.J.2    Wolynes, P.G.3
  • 61
    • 0002006297 scopus 로고
    • Are there pathways for protein folding?
    • Levinthal, C. Are there pathways for protein folding? J. Chim. Phys. 65:44-45, 1968.
    • (1968) J. Chim. Phys. , vol.65 , pp. 44-45
    • Levinthal, C.1
  • 62
    • 0001861319 scopus 로고
    • How to fold graciously
    • DeBrunner, P., Tsibris, J., Munck, E. (eds.). Urbana, IL: University of Illinois Press
    • Levinthal, C. How to fold graciously. In: "Mossbauer Spectroscopy in Biological Systems." DeBrunner, P., Tsibris, J., Munck, E. (eds.). Urbana, IL: University of Illinois Press, 1969:22-24.
    • (1969) Mossbauer Spectroscopy in Biological Systems , pp. 22-24
    • Levinthal, C.1
  • 63
    • 0001538320 scopus 로고
    • Kinetics of proteinlike models: The energy landscape factors that determine folding
    • Betancourt, M.R., Onuchic, J.N. Kinetics of proteinlike models: The energy landscape factors that determine folding. J. Chem. Phys. 103:773-787, 1995.
    • (1995) J. Chem. Phys. , vol.103 , pp. 773-787
    • Betancourt, M.R.1    Onuchic, J.N.2
  • 65
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition
    • Jackson, S.E., Fersht, A.R. Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. Biochemistry 30:10428-10435, 1991.
    • (1991) Biochemistry , vol.30 , pp. 10428-10435
    • Jackson, S.E.1    Fersht, A.R.2
  • 66
    • 0029151158 scopus 로고
    • Submillisecond folding of monomeric X represser
    • Huang, G.S., Oas, T.G. Submillisecond folding of monomeric X represser, Proc. Natl. Acad. Sci. U.S.A. 92:6878-6882, 1995.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 6878-6882
    • Huang, G.S.1    Oas, T.G.2
  • 67
    • 0030584652 scopus 로고    scopus 로고
    • Protein folding triggered by electron transfer
    • Pascher, T., Chesick, J.P., Winkler, J.R., Gray, H.B. Protein folding triggered by electron transfer. Science 271:1558-1560, 1996.
    • (1996) Science , vol.271 , pp. 1558-1560
    • Pascher, T.1    Chesick, J.P.2    Winkler, J.R.3    Gray, H.B.4
  • 68
    • 0029961470 scopus 로고    scopus 로고
    • Equilibrium stability and submillisecond refolding of a designed single-chain arc repressor
    • Robinson, C.R., Sauer, R.T. Equilibrium stability and submillisecond refolding of a designed single-chain arc repressor. Biochemistry 35:13878-13884, 1996.
    • (1996) Biochemistry , vol.35 , pp. 13878-13884
    • Robinson, C.R.1    Sauer, R.T.2
  • 70
    • 0030984109 scopus 로고    scopus 로고
    • Protein folding kinetics exhibit an Arrhenius temperature dependence when corrected for the temperature dependence of protein stability
    • Scalley, M.L., Baker, U. Protein folding kinetics exhibit an Arrhenius temperature dependence when corrected for the temperature dependence of protein stability. Proc. Natl. Acad. Sci. U.S.A. 94:10636-10640, 1997.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 10636-10640
    • Scalley, M.L.1    Baker, U.2
  • 71
    • 0027315969 scopus 로고
    • A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: Verification and refinement of a four-channel model
    • Jennings, P.A., Finn, B.E., Jones, B.E., Matthews, C.R. A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: Verification and refinement of a four-channel model. Biochemistry 32:3783-3789, 1995.
    • (1995) Biochemistry , vol.32 , pp. 3783-3789
    • Jennings, P.A.1    Finn, B.E.2    Jones, B.E.3    Matthews, C.R.4
  • 72
    • 0027715218 scopus 로고
    • Collapse of parallel folding channels in dihydrofolate reductase from Escherichia coli by site-directed mutagenesis
    • Iwakura, M., Jones, B.E., Falzone, C.J., Matthews, C.R. Collapse of parallel folding channels in dihydrofolate reductase from Escherichia coli by site-directed mutagenesis. Biochemistry 32:13566-13574, 1993.
    • (1993) Biochemistry , vol.32 , pp. 13566-13574
    • Iwakura, M.1    Jones, B.E.2    Falzone, C.J.3    Matthews, C.R.4
  • 73
    • 0025146274 scopus 로고
    • Implications of thermodynamics of protein folding for evolution of primary sequences
    • Shakhnovich, E.I., Gutin, A.M. Implications of thermodynamics of protein folding for evolution of primary sequences. Nature 346:773-445, 1990.
    • (1990) Nature , vol.346 , pp. 773-1445
    • Shakhnovich, E.I.1    Gutin, A.M.2
  • 78
    • 0031591390 scopus 로고    scopus 로고
    • Enhanced protein flexibility caused by a destabilizing amino acid replacement in BPTI
    • Beeser, S.A., Goldenberg, D.P., Oas, T.G. Enhanced protein flexibility caused by a destabilizing amino acid replacement in BPTI. J. Mol. Biol. 269:154-164, 1997.
    • (1997) J. Mol. Biol. , vol.269 , pp. 154-164
    • Beeser, S.A.1    Goldenberg, D.P.2    Oas, T.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.