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Volumn 5, Issue 5, 1998, Pages 385-392

Evidence for barrier-limited protein folding kinetics on the microsecond time scale

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C; TRYPTOPHAN;

EID: 0031919973     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0598-385     Document Type: Article
Times cited : (275)

References (57)
  • 2
    • 0031055942 scopus 로고    scopus 로고
    • Kinetic role of early intermediates in protein folding
    • Roder, H. & Colón, 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    Colón, W.2
  • 3
    • 0028174310 scopus 로고
    • How does a protein fold?
    • Sali, A., Shaknovich, E. & Karplus, M. How does a protein fold? Nature 369, 248-251 (1994).
    • (1994) Nature , vol.369 , pp. 248-251
    • Sali, A.1    Shaknovich, E.2    Karplus, M.3
  • 4
    • 0028929556 scopus 로고
    • Principles of protein folding - A perspective from simple exact models
    • Dill, K.A. et al. Principles of protein folding - a perspective from simple exact models. Prot. Sci. 4, 561-602 (1995).
    • (1995) Prot. Sci. , vol.4 , pp. 561-602
    • Dill, K.A.1
  • 5
    • 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
  • 6
    • 0030155292 scopus 로고    scopus 로고
    • Fast-folding experiments and the topography of protein folding energy landscapes
    • Wolynes, P.G., Luthey-Schulten, Z. & Onuchic, J.N. Fast-folding experiments and the topography of protein folding energy landscapes. Chemistry & Biology 3, 425-432 (1996).
    • (1996) Chemistry & Biology , vol.3 , pp. 425-432
    • Wolynes, P.G.1    Luthey-Schulten, Z.2    Onuchic, J.N.3
  • 7
    • 0018368942 scopus 로고
    • Kinetics of the helix-coil transition of a polypeptide with nonionic side groups derived from ultrasonic relaxation measurements
    • Gruenwald, B., Nicola, C.U., Lustig, A., Schwarz, G. & Klump, H. Kinetics of the helix-coil transition of a polypeptide with nonionic side groups derived from ultrasonic relaxation measurements. Biophys. Chem. 9, 137-147 (1979).
    • (1979) Biophys. Chem. , vol.9 , pp. 137-147
    • Gruenwald, B.1    Nicola, C.U.2    Lustig, A.3    Schwarz, G.4    Klump, H.5
  • 8
    • 0030046906 scopus 로고    scopus 로고
    • Fast events in protein folding: Helix melting and formation in a small peptide
    • Williams, S. et al. Fast events in protein folding: helix melting and formation in a small peptide. Biochemistry 35, 691-697 (1996).
    • (1996) Biochemistry , vol.35 , pp. 691-697
    • Williams, S.1
  • 9
    • 0030789351 scopus 로고    scopus 로고
    • Laser temperature jump study of the helix-coil kinetics of an alanine peptide interpreted with a 'kinetic zipper' model
    • Thompson, P.A., Eaton, W.A. & Hofrichter, J. Laser temperature jump study of the helix-coil kinetics of an alanine peptide interpreted with a 'kinetic zipper' model. Biochemistry 36, 9200-9210 (1997).
    • (1997) Biochemistry , vol.36 , pp. 9200-9210
    • Thompson, P.A.1    Eaton, W.A.2    Hofrichter, J.3
  • 10
    • 0038502170 scopus 로고    scopus 로고
    • Folding dynamics and mechanism of β-hairpin formation
    • Muñoz, 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
    • Muñoz, V.1    Thompson, P.A.2    Hofrichter, J.3    Eaton, W.A.4
  • 11
    • 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
  • 12
    • 0027313673 scopus 로고
    • Pathways of protein folding
    • Matthews, C.R. Pathways of protein folding. Annu. Rev. Biochem. 62, 653-683 (1993).
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 653-683
    • Matthews, C.R.1
  • 14
    • 0028082357 scopus 로고
    • Probing the structure of folding intermediates
    • Evans, P.A. & Radford, S.E. Probing the structure of folding intermediates. Curr. Opin. Struct. Biol. 4, 100-106 (1994).
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 100-106
    • Evans, P.A.1    Radford, S.E.2
  • 15
    • 0023669402 scopus 로고
    • Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism. FEBS
    • Kuwajima, K., Yamaya, H., Miwa, S., Sugai, S. & Nagamura, T. Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism. FEBS Lett. 221, 115-118 (1987).
    • (1987) Lett. , vol.221 , pp. 115-118
    • Kuwajima, K.1    Yamaya, H.2    Miwa, S.3    Sugai, S.4    Nagamura, T.5
  • 16
    • 0026781019 scopus 로고
    • Early steps in cytochrome c folding probed by time-resolved circular dichroism and fluorescence spectroscopy
    • Elöve, G.A., Chaffotte, A.F., Roder, H. & Goldberg, M.E. Early steps in cytochrome c folding probed by time-resolved circular dichroism and fluorescence spectroscopy. Biochemistry 31, 6876-6883 (1992).
    • (1992) Biochemistry , vol.31 , pp. 6876-6883
    • Elöve, G.A.1    Chaffotte, A.F.2    Roder, H.3    Goldberg, M.E.4
  • 17
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • Jennings, P.A. & Wright, P.E. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science 262, 892-895 (1993).
    • (1993) Science , vol.262 , pp. 892-895
    • Jennings, P.A.1    Wright, P.E.2
  • 18
    • 0030057477 scopus 로고    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. 3, 193-205 (1996).
    • (1996) Nature Struct. Biol. , vol.3 , pp. 193-205
    • Khorasanizadeh, S.1    Peters, I.D.2    Roder, H.3
  • 20
    • 0031866483 scopus 로고    scopus 로고
    • Amide protection in an early folding intermediate of cytochrome c
    • in the press
    • Sauder, J.M. & Roder, H. Amide protection in an early folding intermediate of cytochrome c. Folding & Design, in the press (1998).
    • (1998) Folding & Design
    • Sauder, J.M.1    Roder, H.2
  • 21
    • 0030664958 scopus 로고    scopus 로고
    • An early intermediate in the folding reaction of the B1 domain of protein G contains a native-like core
    • Park, S.-H., O'Neil, K.T. & Roder, H. An early intermediate in the folding reaction of the B1 domain of protein G contains a native-like core. Biochemistry 36, 14277-14283 (1997).
    • (1997) Biochemistry , vol.36 , pp. 14277-14283
    • Park, S.-H.1    O'Neil, K.T.2    Roder, H.3
  • 23
    • 0029924194 scopus 로고    scopus 로고
    • Further evidence on the equilibrium "pre-molten globule state": Four-state guanidinium chloride-induced unfolding of carbonic anhydrase B at low temperature
    • Uversky, V.N. & Ptitsyn, O.B. Further evidence on the equilibrium "pre-molten globule state": four-state guanidinium chloride-induced unfolding of carbonic anhydrase B at low temperature. J. Mol. Biol. 255, 215-228 (1996).
    • (1996) J. Mol. Biol. , vol.255 , pp. 215-228
    • Uversky, V.N.1    Ptitsyn, O.B.2
  • 24
    • 0028952169 scopus 로고
    • Bipartite structure of the α-lactalbumin molten globule
    • Wu, L.C., Peng, Z.-y. & Kim, P.S. Bipartite structure of the α-lactalbumin molten globule. Nature Struct. Biol. 2, 281-286 (1995).
    • (1995) Nature Struct. Biol. , vol.2 , pp. 281-286
    • Wu, L.C.1    Peng, Z.-Y.2    Kim, P.S.3
  • 25
    • 0000992692 scopus 로고
    • Molten globules: Specific or nonspecific folding intermediates
    • Baldwin, R.L. Molten globules: Specific or nonspecific folding intermediates. Chemtracts: Biochem. Mol. Biol. 2,-379 (1991).
    • (1991) Chemtracts: Biochem. Mol. Biol. , vol.2 , pp. 379
    • Baldwin, R.L.1
  • 26
    • 0028856785 scopus 로고
    • Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications
    • Fersht, A.R. Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications. Proc. Natl. Acad. Sci. USA 92, 10869-10873 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10869-10873
    • Fersht, A.R.1
  • 27
    • 0031026007 scopus 로고    scopus 로고
    • How important is the molten globule for correct folding?
    • Creighton, T.E. How important is the molten globule for correct folding? Trends Biochem. Sci. 22, 6-11 (1997).
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 6-11
    • Creighton, T.E.1
  • 29
    • 0027131947 scopus 로고
    • Fast events in protein folding initiated by nanosecond laser photolysis
    • Jones, C.M. et al. Fast events in protein folding initiated by nanosecond laser photolysis. Proc. Natl. Acad. Sci. USA 90, 11860-11864 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11860-11864
    • Jones, C.M.1
  • 30
    • 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
  • 32
    • 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
  • 34
    • 0031026206 scopus 로고    scopus 로고
    • Folding of cytochrome c initiated by submillisecond mixing
    • Takahashi, S. et al. Folding of cytochrome c initiated by submillisecond mixing. Nature Struct. Biol. 4, 44-50 (1997).
    • (1997) Nature Struct. Biol. , vol.4 , pp. 44-50
    • Takahashi, S.1
  • 35
    • 0031047914 scopus 로고    scopus 로고
    • Submillisecond protein folding kinetics studied by ultrarapid mixing
    • Chan, C.-K. et al. Submillisecond protein folding kinetics studied by ultrarapid mixing. Proc. Natl. Acad. Sci. USA 94, 1779-1784 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1779-1784
    • Chan, C.-K.1
  • 36
    • 0031969090 scopus 로고    scopus 로고
    • A continuous-flow capillary mixer to monitor reactions on the microsecond time scale
    • in the press
    • Shastry, M.C.R., Luck, S.D. & Roder, H. A continuous-flow capillary mixer to monitor reactions on the microsecond time scale. Biophys. J., in the press (1998).
    • (1998) Biophys. J.
    • Shastry, M.C.R.1    Luck, S.D.2    Roder, H.3
  • 37
    • 0023705432 scopus 로고
    • Structural characterization of folding intermediates in cytochrome c by H-exehange labelling and proton NMR
    • Roder, H., Elöve, G.A. & Englander, S.W. Structural characterization of folding intermediates in cytochrome c by H-exehange labelling and proton NMR. Nature 335, 700-704 (1988).
    • (1988) Nature , vol.335 , pp. 700-704
    • Roder, H.1    Elöve, G.A.2    Englander, S.W.3
  • 38
    • 0028352044 scopus 로고
    • Kinetic mechanism of cytochrome c folding: Involvement of the heme and its ligands
    • Elöve, G.A., Bhuyan, A.K. & Roder, H. Kinetic mechanism of cytochrome c folding: involvement of the heme and its ligands. Biochemistry 33, 6925-6935 (1994).
    • (1994) Biochemistry , vol.33 , pp. 6925-6935
    • Elöve, G.A.1    Bhuyan, A.K.2    Roder, H.3
  • 40
    • 0029967474 scopus 로고    scopus 로고
    • Side chain packing of the N- and C-terminal helices plays a critical role in the kinetics of cytochrome c folding
    • Colon, W., Elöve, G.A., Wakem, L.P., Sherman, F. & Roder, H. Side chain packing of the N- and C-terminal helices plays a critical role in the kinetics of cytochrome c folding. Biochemistry 35, 5538-5549 (1996).
    • (1996) Biochemistry , vol.35 , pp. 5538-5549
    • Colon, W.1    Elöve, G.A.2    Wakem, L.P.3    Sherman, F.4    Roder, H.5
  • 42
    • 0028902628 scopus 로고
    • Microsecond generation of oxygen-bound cytochrome c oxidase by rapid solution mixing
    • Takahashi, S., Ching, Y.-c., Wang, J. & Rousseau, D.L. Microsecond generation of oxygen-bound cytochrome c oxidase by rapid solution mixing. J. Biol. Chem. 270, 8405-8407 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 8405-8407
    • Takahashi, S.1    Ching, Y.-C.2    Wang, J.3    Rousseau, D.L.4
  • 43
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein folding: A synthesis
    • Bryngelson, J.D., Onuchic, J.N., Socci, N.D. & Wolynes, P.G. 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, P.G.4
  • 44
    • 0025007598 scopus 로고
    • High-resolution three-dimensional structure of horse heart cytochrome c
    • Bushnell, G.W., Louie, G.V. & Brayer, G.D. High-resolution three-dimensional structure of horse heart cytochrome c. J. Mol. Biol. 214, 585-595 (1990).
    • (1990) J. Mol. Biol. , vol.214 , pp. 585-595
    • Bushnell, G.W.1    Louie, G.V.2    Brayer, G.D.3
  • 45
    • 0026009213 scopus 로고
    • Stable submolecular folding units in a non-compact form of cytochrome c
    • Jeng, M.-F. & Englander, S.W. Stable submolecular folding units in a non-compact form of cytochrome c. J. Mol. Biol. 221, 1045 (1991).
    • (1991) J. Mol. Biol. , vol.221 , pp. 1045
    • Jeng, M.-F.1    Englander, S.W.2
  • 46
    • 0016380496 scopus 로고
    • The Trp-59 fluorescence of ferricytochrome c as a sensitive measure of the over-all protein conformation
    • Tseng, T.Y. The Trp-59 fluorescence of ferricytochrome c as a sensitive measure of the over-all protein conformation. J. Biol. Chem. 249, 1988-1990 (1974).
    • (1974) J. Biol. Chem. , vol.249 , pp. 1988-1990
    • Tseng, T.Y.1
  • 47
    • 0024331090 scopus 로고
    • Structural characterization of protein folding intermediates by proton magnetic resonance and hydrogen exchange
    • Roder, H. Structural characterization of protein folding intermediates by proton magnetic resonance and hydrogen exchange. Meth. Enz. 176, 446-473 (1989).
    • (1989) Meth. Enz. , vol.176 , pp. 446-473
    • Roder, H.1
  • 49
    • 0025179832 scopus 로고
    • Protein Folding
    • Creighton, T.E. Protein Folding. Biochem. J. 270, 1-16 (1990).
    • (1990) Biochem. J. , vol.270 , pp. 1-16
    • Creighton, T.E.1
  • 50
    • 0030816577 scopus 로고    scopus 로고
    • Identification of the predominant non-native histidine ligand in unfolded cytochrome c
    • Colon, W., Wakem, L.P., Sherman, F. & Roder, H. Identification of the predominant non-native histidine ligand in unfolded cytochrome c. Biochemistry 36, 12535-12541 (1997).
    • (1997) Biochemistry , vol.36 , pp. 12535-12541
    • Colon, W.1    Wakem, L.P.2    Sherman, F.3    Roder, H.4
  • 51
    • 0019883235 scopus 로고
    • Nature of the fast and slow refolding reactions of iron(III) cytochrome c
    • Ridge, J.A., Baldwin, R.L. & Labhardt, A.M. Nature of the fast and slow refolding reactions of iron(III) cytochrome c. Biochemistry 20, 1622-1630 (1981).
    • (1981) Biochemistry , vol.20 , pp. 1622-1630
    • Ridge, J.A.1    Baldwin, R.L.2    Labhardt, A.M.3
  • 54
    • 0029964867 scopus 로고    scopus 로고
    • Diffusion-limited contact formation in unfolded cytochrome c: Estimating the maximum rate of protein folding
    • Hagen, S.J., Hofrichter, J., Szabo, A. & Eaton, W.A. Diffusion-limited contact formation in unfolded cytochrome c: Estimating the maximum rate of protein folding. Proc. Natl. Acad. Sci. USA 93, 11615-11617 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11615-11617
    • Hagen, S.J.1    Hofrichter, J.2    Szabo, A.3    Eaton, W.A.4
  • 55
    • 0031043161 scopus 로고    scopus 로고
    • Nucleation mechanisms in protein folding
    • Fersht, A.R. Nucleation mechanisms in protein folding. Curr. Opin. Struct. Biol. 7, 3-9 (1997).
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 3-9
    • Fersht, A.R.1
  • 57
    • 0030473296 scopus 로고    scopus 로고
    • Kinetic intermediates in the formation of the cytochrome c molten globule
    • Colón, W. & Roder, H. Kinetic intermediates in the formation of the cytochrome c molten globule. Nature Struct. Biol. 3, 1019-1025 (1996).
    • (1996) Nature Struct. Biol. , vol.3 , pp. 1019-1025
    • Colón, W.1    Roder, H.2


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