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Volumn 33, Issue 3, 1998, Pages 408-416

Folding-unfolding energy change of a simple sphere model protein and an energy landscape of the folding process

Author keywords

Potential energy curve; Protein folding; Semi empirical calculation; Two state model

Indexed keywords

PROTEIN;

EID: 0032534036     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19981115)33:3<408::AID-PROT9>3.0.CO;2-2     Document Type: Article
Times cited : (6)

References (35)
  • 1
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim, P.S., Baldwin, R.L. Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59:631-660, 1990.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 2
    • 0001756859 scopus 로고
    • Is there a single pathway for the folding of polypeptide chain?
    • Harrison, S.C., Durbin, R. Is there a single pathway for the folding of polypeptide chain? Proc. Natl. Acad. Sci. USA 82:4028-4030, 1985.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4028-4030
    • Harrison, S.C.1    Durbin, R.2
  • 3
    • 0026723063 scopus 로고
    • Protein folding funnels: A kinetic approach to the sequence-structure relationship
    • Leopold, P.E., Montal, M., Onuchic, J.N. Protein folding funnels: A kinetic approach to the sequence-structure relationship. Proc. Natl. Acad. Sci. USA 89:8721-8725, 1992.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8721-8725
    • Leopold, P.E.1    Montal, M.2    Onuchic, J.N.3
  • 4
    • 0029095830 scopus 로고
    • Breathing life into the folding pathway of cytochrome C
    • Kallenbach, N.R. Breathing life into the folding pathway of cytochrome C. Nat. Struct. Biol. 2:813-816, 1995.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 813-816
    • Kallenbach, N.R.1
  • 6
    • 0029018003 scopus 로고
    • Thermodynamics of the temperature-induced unfolding of globular proteins
    • Khechinashvili, N.N., Janin, J., Rodier, F. Thermodynamics of the temperature-induced unfolding of globular proteins. Protein Sci. 4:1315-1324, 1995.
    • (1995) Protein Sci. , vol.4 , pp. 1315-1324
    • Khechinashvili, N.N.1    Janin, J.2    Rodier, F.3
  • 7
    • 0030037083 scopus 로고    scopus 로고
    • Protein folding in the endoplasmic reticulum: Lessons from the human chorionic gonadotropin β subunit
    • Ruddon, R.W., Sherman, S.A., Bedows, E. Protein folding in the endoplasmic reticulum: Lessons from the human chorionic gonadotropin β subunit. Protein Sci. 5:1443-1452, 1996.
    • (1996) Protein Sci. , vol.5 , pp. 1443-1452
    • Ruddon, R.W.1    Sherman, S.A.2    Bedows, E.3
  • 8
    • 0029940033 scopus 로고    scopus 로고
    • Molecular collapse: The rate-limiting step in two-state cytochrome c folding
    • Sosnick, T.R., Mayne, L., Englander, S.W. Molecular collapse: The rate-limiting step in two-state cytochrome c folding. Proteins 24:413-425, 1996.
    • (1996) Proteins , vol.24 , pp. 413-425
    • Sosnick, T.R.1    Mayne, L.2    Englander, S.W.3
  • 9
    • 0029897657 scopus 로고    scopus 로고
    • Direct evidence for a two-state protein unfolding transition from hydrogen-deuterium exchange, mass spectrometry, and NMR
    • Yi, Q., Baker, D. Direct evidence for a two-state protein unfolding transition from hydrogen-deuterium exchange, mass spectrometry, and NMR. Protein Sci. 5:1060-1066, 1996.
    • (1996) Protein Sci. , vol.5 , pp. 1060-1066
    • Yi, Q.1    Baker, D.2
  • 10
    • 0029866436 scopus 로고    scopus 로고
    • Why is protein folding so fast?
    • Baldwin, R.L. Why is protein folding so fast? Proc. Natl. Acad. Sci. USA 93:2627-2628, 1996.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2627-2628
    • Baldwin, R.L.1
  • 11
    • 0030057477 scopus 로고    scopus 로고
    • Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered nucleus 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 nucleus residues. Nat. Struct. Biol. 3:193-205, 1996.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 193-205
    • Khorasanizadeh, S.1    Peters, I.D.2    Roder, H.3
  • 12
    • 0029966342 scopus 로고    scopus 로고
    • Barriers to protein folding: Formation of buried polar interactions is a slow step in acquisition of structure
    • Waldburger, C.D., Jonsson, T., Sauer, R.T. Barriers to protein folding: Formation of buried polar interactions is a slow step in acquisition of structure. Proc. Natl. Acad. Sci. USA 93:2629-2634, 1996.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2629-2634
    • Waldburger, C.D.1    Jonsson, T.2    Sauer, R.T.3
  • 13
    • 0030623529 scopus 로고    scopus 로고
    • Rate of protein folding near the point of thermodynamic equilibrium between the coil and the most stable chain fold
    • Finkelstein, A.V., Badretdinov, A.Y. Rate of protein folding near the point of thermodynamic equilibrium between the coil and the most stable chain fold. Folding Design, 2:115-121, 1997.
    • (1997) Folding Design , vol.2 , pp. 115-121
    • Finkelstein, A.V.1    Badretdinov, A.Y.2
  • 14
    • 0029760326 scopus 로고    scopus 로고
    • Different folding transition states may result in the same native structure
    • Viguera, A.R., Serrano, L., Wilmanns, M. Different folding transition states may result in the same native structure. Nat. Struct. Biol. 3:874-880, 1996.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 874-880
    • Viguera, A.R.1    Serrano, L.2    Wilmanns, M.3
  • 15
    • 0030852463 scopus 로고    scopus 로고
    • Functional rapidly folding proteins from simplified amino acid sequences
    • Riddle, D.S., Santiago, J.V., Bray-Hall, S.T., et al. Functional rapidly folding proteins from simplified amino acid sequences. Nat. Struct. Biol. 4:805-809, 1997.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 805-809
    • Riddle, D.S.1    Santiago, J.V.2    Bray-Hall, S.T.3
  • 16
    • 0030723486 scopus 로고    scopus 로고
    • As simple as can be?
    • Wolynes, P.G. As simple as can be? Nat. Struct. Biol. 4:871-874, 1997.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 871-874
    • Wolynes, P.G.1
  • 17
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill, K.A., Chan, H.S. From Levinthal to pathways to funnels. Nat. Struct. Biol. 4:10-19, 1997.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 19
    • 0003166498 scopus 로고    scopus 로고
    • Protein folding in the landscape perspective: Chevron plots and non-arrhenius kinetics
    • Chan, H.S., Dill, K.A. Protein folding in the landscape perspective: Chevron plots and non-arrhenius kinetics. Proteins 30:2-33, 1998.
    • (1998) Proteins , vol.30 , pp. 2-33
    • Chan, H.S.1    Dill, K.A.2
  • 20
    • 0030606223 scopus 로고    scopus 로고
    • Titration properties and thermodynamics of the transition state for folding: Comparison of two-state and multi-state folding pathways
    • Tan, Y.J., Oliveberg, M., Fersht, A.R. Titration properties and thermodynamics of the transition state for folding: Comparison of two-state and multi-state folding pathways. J. Mol. Biol. 264:377-389, 1996.
    • (1996) J. Mol. Biol. , vol.264 , pp. 377-389
    • Tan, Y.J.1    Oliveberg, M.2    Fersht, A.R.3
  • 22
    • 0028868995 scopus 로고
    • The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering method: Evidence for a nucleation-condensation mechanism for protein folding
    • Itzhaki, L.S., Otzen, D.E., Fersht, A.R. The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering method: Evidence for a nucleation-condensation mechanism for protein folding. J. Mol. Biol. 254:260-288, 1995.
    • (1995) J. Mol. Biol. , vol.254 , pp. 260-288
    • Itzhaki, L.S.1    Otzen, D.E.2    Fersht, A.R.3
  • 24
    • 0001313268 scopus 로고    scopus 로고
    • Potential of mean force calculation of solute molecules in water by a modified solvent-accessible surface method
    • Fukunishi, Y., Suzuki, M. Potential of mean force calculation of solute molecules in water by a modified solvent-accessible surface method. J. Comput. Chem. 18:1656-1663, 1997.
    • (1997) J. Comput. Chem. , vol.18 , pp. 1656-1663
    • Fukunishi, Y.1    Suzuki, M.2
  • 25
    • 0003766353 scopus 로고
    • Hydrogen bonding in biological macromolecules
    • Berlin: Springer-Verlag
    • Jeffrey, G.A., Saenger, W. (eds.). Hydrogen bonding in biological macromolecules. In: "Hydrogen Bonding in Biological Structures." Berlin: Springer-Verlag, 1991:307-422.
    • (1991) Hydrogen Bonding in Biological Structures , pp. 307-422
    • Jeffrey, G.A.1    Saenger, W.2
  • 26
    • 20644431615 scopus 로고
    • Theory of solutions of molecules containing widely separated charges with special application to zwitterions
    • Kirkwood, J.G. Theory of solutions of molecules containing widely separated charges with special application to zwitterions. J. Chem. Phys. 2:351-361, 1934.
    • (1934) J. Chem. Phys. , vol.2 , pp. 351-361
    • Kirkwood, J.G.1
  • 27
    • 33947468892 scopus 로고
    • Theory of protein titration curves. I. General equations for impenetrable spheres
    • Tanford, C., Kirkwood, J.G. Theory of protein titration curves. I. General equations for impenetrable spheres. J. Am. Chem. Soc. 79:5333-5339, 1957.
    • (1957) J. Am. Chem. Soc. , vol.79 , pp. 5333-5339
    • Tanford, C.1    Kirkwood, J.G.2
  • 28
    • 0001205818 scopus 로고
    • Electrostatic effect in water-accessible regions of proteins
    • Mehler, E.L., Eichele, G. Electrostatic effect in water-accessible regions of proteins. Biochemistry 23:3887-3891, 1984.
    • (1984) Biochemistry , vol.23 , pp. 3887-3891
    • Mehler, E.L.1    Eichele, G.2
  • 29
    • 0022596727 scopus 로고
    • Solvation energy in protein folding and binding
    • Eisenberg, D., McLachlan, A.D. Solvation energy in protein folding and binding. Nature 319:199-201, 1986.
    • (1986) Nature , vol.319 , pp. 199-201
    • Eisenberg, D.1    McLachlan, A.D.2
  • 30
    • 0023338543 scopus 로고
    • Accessible surface area as a measure of the thermodynamic parameters of hydration of peptides
    • Ooi, T., Obatake, T., Nemethy, G., Scheraga, H.A. Accessible surface area as a measure of the thermodynamic parameters of hydration of peptides. Proc. Natl. Acad. Sci. USA 84:3086-3091, 1987.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3086-3091
    • Ooi, T.1    Obatake, T.2    Nemethy, G.3    Scheraga, H.A.4
  • 31
    • 0028863592 scopus 로고
    • Atomic solvation parameter in the analysis of protein-protein docking results
    • Cumming, M.D., Hart, T.N., Read, R.J. Atomic solvation parameter in the analysis of protein-protein docking results. Protein Sci. 4:2087-2099, 1995.
    • (1995) Protein Sci. , vol.4 , pp. 2087-2099
    • Cumming, M.D.1    Hart, T.N.2    Read, R.J.3
  • 32
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interface
    • Wimley, W.C., White, S.H. Experimentally determined hydrophobicity scale for proteins at membrane interface. Nat. Struct. Biol. 3:842-848, 1996.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 33
    • 0029900846 scopus 로고    scopus 로고
    • The magnitude of the backbone conformational entropy change in protein folding
    • D'Aquino, A.J., Gomez, J., Hilser, V.J., Lee, K.H., Amzel, L.M., Freire, E. The magnitude of the backbone conformational entropy change in protein folding. Proteins 25:143-156, 1996.
    • (1996) Proteins , vol.25 , pp. 143-156
    • D'Aquino, A.J.1    Gomez, J.2    Hilser, V.J.3    Lee, K.H.4    Amzel, L.M.5    Freire, E.6
  • 34
    • 0030945036 scopus 로고    scopus 로고
    • Consistency in structural energies of protein folding and peptide recognition
    • Zhang, C., Cornette, J.L., Delisi, C. Consistency in structural energies of protein folding and peptide recognition. Protein Sci. 6:1057-1064, 1997.
    • (1997) Protein Sci. , vol.6 , pp. 1057-1064
    • Zhang, C.1    Cornette, J.L.2    Delisi, C.3
  • 35
    • 0001229923 scopus 로고
    • Molecular dynamics study of the dependence of water solvation free energy on solute curvature and surface area
    • Wallqvist, A., Berne, B.J. Molecular dynamics study of the dependence of water solvation free energy on solute curvature and surface area. J. Phys. Chem. 99:2885-2893, 1995.
    • (1995) J. Phys. Chem. , vol.99 , pp. 2885-2893
    • Wallqvist, A.1    Berne, B.J.2


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