메뉴 건너뛰기




Volumn 289, Issue 5, 1999, Pages 1459-1467

Folding mechanism of Pseudomonas aeruginosa cytochrome c551: Role of electrostatic interactions on the hydrophobic collapse and transition state properties

Author keywords

Burst phase; Folding kinetics; pH effect; Transition state

Indexed keywords

CYTOCHROME C; GLUTAMIC ACID; HISTIDINE; IRON; LYSINE; TRYPTOPHAN;

EID: 0033603397     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2852     Document Type: Article
Times cited : (23)

References (40)
  • 1
    • 0028024928 scopus 로고
    • Specific nucleus as the transition state for protein folding: Evidence from the lattice model
    • Abkevich V. I., Gutin A. M., Shakhnovich E. I. Specific nucleus as the transition state for protein folding: evidence from the lattice model. Biochemistry. 33:1994;10026-10036.
    • (1994) Biochemistry , vol.33 , pp. 10026-10036
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 2
    • 0030347877 scopus 로고    scopus 로고
    • On-pathway versus off-pathway folding intermediates
    • Baldwin R. L. On-pathway versus off-pathway folding intermediates. Fold. Des. 1:1996;R1-R8.
    • (1996) Fold. Des. , vol.1
    • Baldwin, R.L.1
  • 4
    • 0024726838 scopus 로고
    • Determination of the dead-time of a stopped-flow fluorometer
    • Brissette P., Ballou D. P., Massey V. Determination of the dead-time of a stopped-flow fluorometer. Anal. Biochem. 181:1989;234-238.
    • (1989) Anal. Biochem. , vol.181 , pp. 234-238
    • Brissette, P.1    Ballou, D.P.2    Massey, V.3
  • 7
    • 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: Struct. Funct. Genet. 30:1998;2-33.
    • (1998) Proteins: Struct. Funct. Genet. , vol.30 , pp. 2-33
    • Chan, H.S.1    Dill, K.A.2
  • 8
    • 0022399830 scopus 로고
    • Helix movements and the reconstruction of the haem pocket during the evolution of the cytochrome c family
    • Chothia C., Lesk A. M. Helix movements and the reconstruction of the haem pocket during the evolution of the cytochrome c family. J. Mol. Biol. 182:1985;151-158.
    • (1985) J. Mol. Biol. , vol.182 , pp. 151-158
    • Chothia, C.1    Lesk, A.M.2
  • 9
    • 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
    • Colón 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. 35:1996;5538-5549.
    • (1996) Biochemistry , vol.35 , pp. 5538-5549
    • Colón, W.1    Elöve, G.A.2    Wakem, L.P.3    Sherman, F.4    Roder, H.5
  • 10
    • 0030816577 scopus 로고    scopus 로고
    • Identification of the predominant non-native histidine ligand in unfolded cytochrome c
    • Colón W., Wakem L. P., Sherman F., Roder H. Identification of the predominant non-native histidine ligand in unfolded cytochrome c. Biochemistry. 36:1997;12535-12541.
    • (1997) Biochemistry , vol.36 , pp. 12535-12541
    • Colón, W.1    Wakem, L.P.2    Sherman, F.3    Roder, H.4
  • 13
    • 0030726758 scopus 로고    scopus 로고
    • Populating the equilibrium molten globule state of apomyoglobin under conditions suitable for characterization by NMR
    • Eliezer D., Jennings P. A., Dyson H. J., Wright P. E. Populating the equilibrium molten globule state of apomyoglobin under conditions suitable for characterization by NMR. FEBS Letters. 417:1997;92-96.
    • (1997) FEBS Letters , vol.417 , pp. 92-96
    • Eliezer, D.1    Jennings, P.A.2    Dyson, H.J.3    Wright, P.E.4
  • 14
    • 0031043161 scopus 로고    scopus 로고
    • Nucleation mechanism in protein folding
    • Fersht A. R. Nucleation mechanism in protein folding. Curr. Opin. Struct. Biol. 7:1997;3-9.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 3-9
    • Fersht, A.R.1
  • 15
    • 0028944346 scopus 로고
    • Is burst hydrophobic collapse necessary for protein folding?
    • Gutin A. M., Abkevich V. I., Shakhnovich E. I. Is burst hydrophobic collapse necessary for protein folding? Biochemistry. 34:1995;3066-3076.
    • (1995) Biochemistry , vol.34 , pp. 3066-3076
    • Gutin, A.M.1    Abkevich, V.I.2    Shakhnovich, E.I.3
  • 16
    • 0032488914 scopus 로고    scopus 로고
    • Cytochrome c folding traps are not due solely to histidine heme ligation: Direct demonstration of a role for N-terminal amino group heme ligation
    • Hammack B., Godbole S., Bowler B. E. Cytochrome c folding traps are not due solely to histidine heme ligation: direct demonstration of a role for N-terminal amino group heme ligation. J. Mol. Biol. 275:1998;719-724.
    • (1998) J. Mol. Biol. , vol.275 , pp. 719-724
    • Hammack, B.1    Godbole, S.2    Bowler, B.E.3
  • 17
    • 0032536194 scopus 로고    scopus 로고
    • Group additive contributions to the alcohol-induced α-helix formation of melittin: Implications for the mechanism of the alcohol effects on proteins
    • Hirota N., Mizuno K., Goto Y. Group additive contributions to the alcohol-induced α-helix formation of melittin: implications for the mechanism of the alcohol effects on proteins. J. Mol. Biol. 275:1998;365-378.
    • (1998) J. Mol. Biol. , vol.275 , pp. 365-378
    • Hirota, N.1    Mizuno, K.2    Goto, Y.3
  • 18
    • 0026587310 scopus 로고
    • Cooperative interactions during protein folding
    • Horovitz A., Fersht A. R. Cooperative interactions during protein folding. J. Mol. Biol. 224:1992;733-740.
    • (1992) J. Mol. Biol. , vol.224 , pp. 733-740
    • Horovitz, A.1    Fersht, A.R.2
  • 20
    • 0026516420 scopus 로고
    • Kinetic coupling between protein folding and prolyl isomerization. I. Theoretical models
    • Kiefhaber T., Kohler H. H., Schmid F. X. Kinetic coupling between protein folding and prolyl isomerization. I. Theoretical models. J. Mol. Biol. 224:1992;217-229.
    • (1992) J. Mol. Biol. , vol.224 , pp. 217-229
    • Kiefhaber, T.1    Kohler, H.H.2    Schmid, F.X.3
  • 21
    • 0028926855 scopus 로고
    • A native tertiary interaction stabilizes the A state of cytochrome c
    • Marmorino J. L., Pielak G. J. A native tertiary interaction stabilizes the A state of cytochrome c. Biochemistry. 34:1995;3140-3143.
    • (1995) Biochemistry , vol.34 , pp. 3140-3143
    • Marmorino, J.L.1    Pielak, G.J.2
  • 22
  • 23
    • 0020004138 scopus 로고
    • 551from Pseudomonasaeruginosa refined at 1.6 Å resolution and comparison of the two redox forms
    • 551from Pseudomonasaeruginosa refined at 1.6 Å resolution and comparison of the two redox forms. J. Mol. Biol. 156:1982;389-409.
    • (1982) J. Mol. Biol. , vol.156 , pp. 389-409
    • Matsuura, Y.1    Takano, T.2    Dickerson, R.E.3
  • 24
    • 0031862845 scopus 로고    scopus 로고
    • Refolding rate of stability enhanced cytochrome c is independent of thermodynamic driving force
    • McGee W. A., Nall B. T. Refolding rate of stability enhanced cytochrome c is independent of thermodynamic driving force. Protein Sci. 7:1998;1071-1082.
    • (1998) Protein Sci. , vol.7 , pp. 1071-1082
    • McGee, W.A.1    Nall, B.T.2
  • 27
    • 0025420076 scopus 로고
    • Measuring and increasing protein stability
    • Pace C. N. Measuring and increasing protein stability. Trends Biotechnol. 8:1990;93-98.
    • (1990) Trends Biotechnol. , vol.8 , pp. 93-98
    • Pace, C.N.1
  • 28
    • 0028791393 scopus 로고
    • An integrated kinetic analysis of intermediates and transition states in protein folding reactions
    • Parker M. J., Spencer J., Clarke A. R. An integrated kinetic analysis of intermediates and transition states in protein folding reactions. J. Mol. Biol. 253:1995;771-786.
    • (1995) J. Mol. Biol. , vol.253 , pp. 771-786
    • Parker, M.J.1    Spencer, J.2    Clarke, A.R.3
  • 29
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and refolding rates of single domain proteins
    • Plaxco K. W., Simons K. T., Baker D. Contact order, transition state placement and refolding rates of single domain proteins. J. Mol. Biol. 277:1998;985-994.
    • (1998) J. Mol. Biol. , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 30
    • 0032496419 scopus 로고    scopus 로고
    • Protein folding and protein evolution: Common folding nucleus in different subfamilies of c -type cytochromes?
    • Ptitsyn O. B. Protein folding and protein evolution: common folding nucleus in different subfamilies of c -type cytochromes? J. Mol. Biol. 278:1998;655-666.
    • (1998) J. Mol. Biol. , vol.278 , pp. 655-666
    • Ptitsyn, O.B.1
  • 31
    • 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. 7:1997;15-28.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 15-28
    • Roder, H.1    Colón, W.2
  • 32
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants
    • Santoro M. M., Bolen D. W. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants. Biochemistry. 27:1988;8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 34
    • 0030958760 scopus 로고    scopus 로고
    • Transient aggregates in protein folding are easily mistaken for folding intermediates
    • Silow M., Oliveberg M. Transient aggregates in protein folding are easily mistaken for folding intermediates. Proc. Natl Acad. Sci. USA. 94:1997;6084-6086.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 6084-6086
    • Silow, M.1    Oliveberg, M.2
  • 35
    • 0031919973 scopus 로고    scopus 로고
    • Evidence for barrier-limited protein folding kinetics on the microsecond time scale
    • Shastry R. M. C., Roder H. Evidence for barrier-limited protein folding kinetics on the microsecond time scale. Nature Struct. Biol. 5:1998;385-392.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 385-392
    • Shastry, R.M.C.1    Roder, H.2
  • 39
    • 0031662891 scopus 로고    scopus 로고
    • Evidence for an unfolding and refolding pathway in cytochrome c
    • Xu Y., Mayne L., Englander S. W. Evidence for an unfolding and refolding pathway in cytochrome c. Nature Struct. Biol. 5:1998;774-778.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 774-778
    • Xu, Y.1    Mayne, L.2    Englander, S.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.