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Volumn 401, Issue 6751, 1999, Pages 400-403

Interpreting the folding kinetics of helical proteins

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; KINETICS; MODEL; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; STRUCTURE ANALYSIS; THERMODYNAMICS;

EID: 0033598375     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/43940     Document Type: Article
Times cited : (258)

References (30)
  • 2
    • 0344301982 scopus 로고    scopus 로고
    • Protein folding: A perspective from theory and experiment
    • Dobson, D. M., Šali, A. & Karplus, M. Protein folding: A perspective from theory and experiment. Angew. Chem. Int. Ed. 37, 865-893 (1998).
    • (1998) Angew. Chem. Int. Ed. , vol.37 , pp. 865-893
    • Dobson, D.M.1    Šali, A.2    Karplus, M.3
  • 3
    • 0031787022 scopus 로고    scopus 로고
    • 100,000 protein structures for the biologist
    • Šali, A. 100,000 protein structures for the biologist. Nature Struct. Biol. 5, 1029-1032 (1998).
    • (1998) Nature Struct. Biol. , vol.5 , pp. 1029-1032
    • Šali, A.1
  • 4
    • 0030626588 scopus 로고    scopus 로고
    • The Levinthal paradox: Yesterday and today
    • Karplus, M. The Levinthal paradox: yesterday and today. Fold. Des. 2, 569-576 (1997).
    • (1997) Fold. Des. , vol.2 , pp. 569-576
    • Karplus, M.1
  • 5
    • 0028949547 scopus 로고
    • Theoretical studies of protein folding and unfolding
    • Karplus, M. & Šali, A. Theoretical studies of protein folding and unfolding. Curr. Opin. Struct. Biol. 5, 58-73 (1995).
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 58-73
    • Karplus, M.1    Šali, A.2
  • 6
    • 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
  • 7
    • 0032147243 scopus 로고    scopus 로고
    • Protein folding mechanisms and the multidimensional folding funnel
    • Socci, N. D., Onuchic, J. N. & Wolynes, P. G. Protein folding mechanisms and the multidimensional folding funnel. Proteins 32, 136-158 (1998).
    • (1998) Proteins , vol.32 , pp. 136-158
    • Socci, N.D.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 8
    • 0017251893 scopus 로고
    • Protein-folding dynamics
    • Karplus, M. & Weaver, D. L. Protein-folding dynamics. Nature 260, 404-406 (1976).
    • (1976) Nature , vol.260 , pp. 404-406
    • Karplus, M.1    Weaver, D.L.2
  • 9
    • 0028143603 scopus 로고
    • Characterization of the transition state of protein unfolding by use of molecular dynamics: Chymotrypsin inhibitor 2
    • Li, A. & Daggett, V. Characterization of the transition state of protein unfolding by use of molecular dynamics: chymotrypsin inhibitor 2. Proc. Natl Acad. Sci. USA 91, 10430-10434 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10430-10434
    • Li, A.1    Daggett, V.2
  • 10
    • 0029124153 scopus 로고
    • Acid and thermal denaturation of Barnase investigated by molecular dynamics simulations
    • Caflisch, A. & Karplus, M. Acid and thermal denaturation of Barnase investigated by molecular dynamics simulations. J. Mol. Biol. 252, 672-708 (1995).
    • (1995) J. Mol. Biol. , vol.252 , pp. 672-708
    • Caflisch, A.1    Karplus, M.2
  • 11
    • 0029151245 scopus 로고
    • First principles calculation of the folding free energy of a three-helix bundle protein
    • Boczko, E. M. & Brooks, C. L. III. 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. III2
  • 12
    • 0030967896 scopus 로고    scopus 로고
    • Boczko, E. M. Exploring the folding free energy surface of a three-helix bundle protein
    • Guo, Z. Y., Brooks, C. L. III. & Boczko, E. M. Exploring the folding free energy surface of a three-helix bundle protein. Proc. Natl Acad Sci. USA 94, 10161-10166 (1997).
    • (1997) Proc. Natl Acad Sci. USA , vol.94 , pp. 10161-10166
    • Guo, Z.Y.1    Brooks C.L. III2
  • 13
    • 0032561237 scopus 로고    scopus 로고
    • Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solution
    • Duan, Y. & Kollman, P. A. Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solution. Science 282, 707-744 (1998).
    • (1998) Science , vol.282 , pp. 707-744
    • Duan, Y.1    Kollman, P.A.2
  • 14
    • 0026801084 scopus 로고
    • Three-dimensional solution structure of the B domain of Staphylococcal protein A: Comparisons of the solution and crystal structures
    • Gouda, H. et al. Three-dimensional solution structure of the B domain of Staphylococcal protein A: Comparisons of the solution and crystal structures. Biochemistry 31, 9665-9672 (1992).
    • (1992) Biochemistry , vol.31 , pp. 9665-9672
    • Gouda, H.1
  • 15
    • 0033613906 scopus 로고    scopus 로고
    • Native proteins are surface-molten solids: Application of the Lindemann criterion for the solid versus liquid state
    • Zhou, Y., Vitkup, D. & Karplus, M. Native proteins are surface-molten solids: Application of the Lindemann criterion for the solid versus liquid state. J. Mol. Biol. 285, 1371-1375 (1999).
    • (1999) J. Mol. Biol. , vol.285 , pp. 1371-1375
    • Zhou, Y.1    Vitkup, D.2    Karplus, M.3
  • 16
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn, O. B. Molten globule and protein folding. Adv. Protein Chem. 47, 83-230 (1995).
    • (1995) Adv. Protein Chem. , vol.47 , pp. 83-230
    • Ptitsyn, O.B.1
  • 17
    • 0018588511 scopus 로고
    • Stability of proteins: Small globular proteins
    • Privalov, P. L. Stability of proteins: Small globular proteins. Adv. Protein Chem. 33, 167-241 (1979).
    • (1979) Adv. Protein Chem. , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 18
    • 0031475159 scopus 로고    scopus 로고
    • Folding thermodynamics of a model three-helix bundle protein
    • Zhou, Y. & Karplus, M. Folding thermodynamics of a model three-helix bundle protein. Proc. Natl Acad. Sci. USA 94, 14429-14432 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 14429-14432
    • Zhou, Y.1    Karplus, M.2
  • 19
    • 0030770294 scopus 로고    scopus 로고
    • Oligomer formation by 3D domain swapping: A model for protein assembly and misassembly
    • Schlunegger, M., Bennett, M. & Eisenberg, D. Oligomer formation by 3D domain swapping: A model for protein assembly and misassembly. Adv. Protein Chem. 50, 61-122 (1997).
    • (1997) Adv. Protein Chem. , vol.50 , pp. 61-122
    • Schlunegger, M.1    Bennett, M.2    Eisenberg, D.3
  • 20
    • 0031465967 scopus 로고    scopus 로고
    • Multiple unfolding simulations reconcile the "new new" of protein folding with the old
    • Lazaridis, T. & Karplus, M. Multiple unfolding simulations reconcile the "new new" of protein folding with the old. Science 278, 1928-1931 (1997).
    • (1997) Science , vol.278 , pp. 1928-1931
    • Lazaridis, T.1    Karplus, M.2
  • 21
    • 0031055942 scopus 로고    scopus 로고
    • Kinetic role of early intermediates in protein folding
    • Roder, H. & Colon, W. Kinetic role of early intermediates in protein folding. Curr. Opin. Struct. Biol. 7, 15-28 (1997).
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 15-28
    • Roder, H.1    Colon, W.2
  • 22
    • 0032574827 scopus 로고    scopus 로고
    • Dynamics and function of proteins: The search for general concepts
    • Frauenfelder, H. & McMahon, B. Dynamics and function of proteins: The search for general concepts. Proc. Natl Acad. Sci. USA 95, 4795-4797 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 4795-4797
    • Frauenfelder, H.1    McMahon, B.2
  • 23
    • 0032554626 scopus 로고    scopus 로고
    • Protein folding dynamics - Quantitative comparison between theory and experiment
    • Burton, R. E., Myers, J. K. & Oas, T. G. Protein folding dynamics - quantitative comparison between theory and experiment. Biochemistry 37, 5337-5343 (1998).
    • (1998) Biochemistry , vol.37 , pp. 5337-5343
    • Burton, R.E.1    Myers, J.K.2    Oas, T.G.3
  • 24
    • 0033534586 scopus 로고    scopus 로고
    • Effect of H helix destabilizing mutations on the kinetic and equilibrium folding of apomyoglobin
    • Cavagnero, S., Dyson, H. J. & Wright, P. E. Effect of H helix destabilizing mutations on the kinetic and equilibrium folding of apomyoglobin. J. Mol. Biol. 285, 269-282 (1999).
    • (1999) J. Mol. Biol. , vol.285 , pp. 269-282
    • Cavagnero, S.1    Dyson, H.J.2    Wright, P.E.3
  • 25
    • 0033548553 scopus 로고    scopus 로고
    • Rapid folding with and without populated intermediates in the homologous four-helix proteins Im7 and Im9
    • Ferguson, N., Capaldi, A. P. Jerrez, R., Kleanthous, C. & Radford, S. E. Rapid folding with and without populated intermediates in the homologous four-helix proteins Im7 and Im9. J. Mol. Biol. 286, 1597-1608 (1999).
    • (1999) J. Mol. Biol. , vol.286 , pp. 1597-1608
    • Ferguson, N.1    Capaldi, A.P.2    Jerrez, R.3    Kleanthous, C.4    Radford, S.E.5
  • 26
    • 0016696599 scopus 로고
    • Studies on protein folding, unfolding and fluctuation? by computer simulations
    • Taketomi, H., Ueda, Y. & Gǒ, N. Studies on protein folding, unfolding and fluctuation? by computer simulations. Int. J. Pept. Protein Res. 7, 445-459 (1975).
    • (1975) Int. J. Pept. Protein Res. , vol.7 , pp. 445-459
    • Taketomi, H.1    Ueda, Y.2    Gǒ, N.3
  • 27
    • 33646987405 scopus 로고
    • Optimized Monte Carlo data analysis
    • Ferrenberg, A. M. & Swendsen, R. H. Optimized Monte Carlo data analysis. Phys. Rev. Lett. 63, 1195-1197 (1989).
    • (1989) Phys. Rev. Lett. , vol.63 , pp. 1195-1197
    • Ferrenberg, A.M.1    Swendsen, R.H.2
  • 28
    • 0001015060 scopus 로고    scopus 로고
    • Equilibrium thermodynamics of homopolymers and clusters: Molecular dynamics and Monte Carlo simulations of systems with square well interactions
    • Zhou, Y., Karplus, M., Wichert, J. M. & Hall, C. K. Equilibrium thermodynamics of homopolymers and clusters: Molecular dynamics and Monte Carlo simulations of systems with square well interactions. J. Chem. Phys. 107, 10691-10708 (1997).
    • (1997) J. Chem. Phys. , vol.107 , pp. 10691-10708
    • Zhou, Y.1    Karplus, M.2    Wichert, J.M.3    Hall, C.K.4
  • 29
    • 0029973119 scopus 로고    scopus 로고
    • Direct observation of fast protein folding: The initial collapse of apomyoglobin
    • Ballew, R. M., Sabelko, J. & Gruebele, M. Direct observation of fast protein folding: The initial collapse of apomyoglobin. Proc. Natl Acad. Sci. USA 93, 5759-5764 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 5759-5764
    • Ballew, R.M.1    Sabelko, J.2    Gruebele, M.3
  • 30
    • 0038502170 scopus 로고    scopus 로고
    • Folding dynamics and mechanism of β-hairpin formation
    • Munoz, V., Thompson, P. A., Hofrichter, J. & Eaton, W. A. Folding dynamics and mechanism of β-hairpin formation. Nature 390, 196-199 (1997).
    • (1997) Nature , vol.390 , pp. 196-199
    • Munoz, V.1    Thompson, P.A.2    Hofrichter, J.3    Eaton, W.A.4


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