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Volumn 46, Issue 12, 2007, Pages 3925-3932

Pathway of oxidative folding of bovine α-interferon: Predominance of native disulfide-bonded folding intermediates

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ISOMERS; MATHEMATICAL MODELS; MOLECULAR STRUCTURE; OXIDATION; POLYPEPTIDES;

EID: 33947704135     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0623126     Document Type: Article
Times cited : (9)

References (29)
  • 1
    • 0037221599 scopus 로고    scopus 로고
    • Is there a unifying mechanism for protein folding?
    • Daggett, V., and Fersht, A. R. (2003) Is there a unifying mechanism for protein folding? Trends Biochem. Sci. 28, 18-25.
    • (2003) Trends Biochem. Sci , vol.28 , pp. 18-25
    • Daggett, V.1    Fersht, A.R.2
  • 2
    • 0020024242 scopus 로고
    • Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding
    • Kim, P. S., and Baldwin, R. L. (1982) Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding, Annu. Rev. Biochem. 51, 459-489.
    • (1982) Annu. Rev. Biochem , vol.51 , pp. 459-489
    • Kim, P.S.1    Baldwin, R.L.2
  • 3
    • 0023626273 scopus 로고
    • Protein folding: Hypotheses and experiments
    • Ptitsyn, O. B. (1987) Protein folding: Hypotheses and experiments, J. Protein Chem. 6, 273-293.
    • (1987) J. Protein Chem , vol.6 , pp. 273-293
    • Ptitsyn, O.B.1
  • 4
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim, P. S., and Baldwin, R. L. (1990) Intermediates in the folding reactions of small proteins, Annu. Rev. Biochem. 59, 631-660.
    • (1990) Annu. Rev. Biochem , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 5
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • Kauzmann, W. (1959) Some factors in the interpretation of protein denaturation, Adv. Protein Chem. 14, 1-63.
    • (1959) Adv. Protein Chem , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 6
    • 0038519321 scopus 로고
    • Contribution of hydrophobic interactions to the stability of globular confirmation of proteins
    • Tanford, C. (1962) Contribution of hydrophobic interactions to the stability of globular confirmation of proteins, J. Am. Chem. Soc. 84, 4240-4247.
    • (1962) J. Am. Chem. Soc , vol.84 , pp. 4240-4247
    • Tanford, C.1
  • 7
    • 0024391879 scopus 로고
    • How does protein folding get started?
    • Baldwin, R. L. (1989) How does protein folding get started? Trends Biochem. Sci. 14, 291-294.
    • (1989) Trends Biochem. Sci , vol.14 , pp. 291-294
    • Baldwin, R.L.1
  • 8
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill, K. A. (1990) Dominant forces in protein folding, Biochemistry 29, 7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 9
    • 0037181484 scopus 로고    scopus 로고
    • The chicken-egg scenario of protein folding revisited
    • Uversky, V. N., and Fink, A. L. (2002) The chicken-egg scenario of protein folding revisited, FEBS Lett. 515, 79-83.
    • (2002) FEBS Lett , vol.515 , pp. 79-83
    • Uversky, V.N.1    Fink, A.L.2
  • 10
    • 0029053552 scopus 로고
    • Folding of a Nascent Polypeptide Chain in vitro: Cooperative Formation of Structure in a Protein Module
    • de Prat Gay, G., Ruiz-Sanz, J., Neira, J. L., Itzhaki, L. S., and Fersh, A. R. (1995) Folding of a Nascent Polypeptide Chain in vitro: Cooperative Formation of Structure in a Protein Module, Proc. Natl. Acad. Sci. U.S.A. 92, 3683-3686.
    • (1995) Proc. Natl. Acad. Sci. U.S.A , vol.92 , pp. 3683-3686
    • de Prat Gay, G.1    Ruiz-Sanz, J.2    Neira, J.L.3    Itzhaki, L.S.4    Fersh, A.R.5
  • 11
    • 0028856785 scopus 로고
    • Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications
    • Fersht, A. R. (1995) Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications, Proc. Natl. Acad. Sci. U.S.A. 92, 10869-10873.
    • (1995) Proc. Natl. Acad. Sci. U.S.A , vol.92 , pp. 10869-10873
    • Fersht, A.R.1
  • 12
    • 0027434035 scopus 로고
    • The disulfide folding pathway of hirudin elucidated by stop/go folding experiments
    • Chatrenet, B., and Chang, J.-Y. (1993) The disulfide folding pathway of hirudin elucidated by stop/go folding experiments, J. Biol. Chem. 268, 20988-20996.
    • (1993) J. Biol. Chem , vol.268 , pp. 20988-20996
    • Chatrenet, B.1    Chang, J.-Y.2
  • 13
    • 0028303047 scopus 로고
    • Controlling the speed of hirudin folding
    • Chang, J.-Y. (1994) Controlling the speed of hirudin folding, Biochem. J. 300, 643-650.
    • (1994) Biochem. J , vol.300 , pp. 643-650
    • Chang, J.-Y.1
  • 14
    • 0028121986 scopus 로고
    • The disulfide folding pathway of potato carboxy-peptidase inhibitor
    • Chang, J.-Y., Cannals, F., Schindler, P., Querol, E., and Aviles, F. X. (1994) The disulfide folding pathway of potato carboxy-peptidase inhibitor, J. Biol. Chem. 269, 22087-22094.
    • (1994) J. Biol. Chem , vol.269 , pp. 22087-22094
    • Chang, J.-Y.1    Cannals, F.2    Schindler, P.3    Querol, E.4    Aviles, F.X.5
  • 15
    • 30644469614 scopus 로고    scopus 로고
    • Fully oxidized scrambled isomers are essential and predominant folding intermediates of cardiotoxin-III
    • Chang, J.-Y., Lu, B.-Y., Lin, C., and Yu, C. (2006) Fully oxidized scrambled isomers are essential and predominant folding intermediates of cardiotoxin-III, FEBS Lett. 580, 656-660.
    • (2006) FEBS Lett , vol.580 , pp. 656-660
    • Chang, J.-Y.1    Lu, B.-Y.2    Lin, C.3    Yu, C.4
  • 18
    • 0031566032 scopus 로고    scopus 로고
    • The three-dimensional high resolution structure of human interferon α-2a determined by heteronuclear NMR spectroscopy in solution
    • Klaus, W., Gsell, B., Labhardt, A. M., Wipf, B., and Senn, H. (1997) The three-dimensional high resolution structure of human interferon α-2a determined by heteronuclear NMR spectroscopy in solution, J. Mol. Biol. 274, 661-675.
    • (1997) J. Mol. Biol , vol.274 , pp. 661-675
    • Klaus, W.1    Gsell, B.2    Labhardt, A.M.3    Wipf, B.4    Senn, H.5
  • 19
    • 0019428529 scopus 로고
    • Assignment of the disulphide bonds of leukocyte interferon
    • Wetzel, R. (1981) Assignment of the disulphide bonds of leukocyte interferon, Nature 289, 606-607.
    • (1981) Nature , vol.289 , pp. 606-607
    • Wetzel, R.1
  • 20
    • 0022555899 scopus 로고
    • Disulfide bonds as probes of protein folding pathways
    • Creighton, T. E. (1986) Disulfide bonds as probes of protein folding pathways, Methods Enzymol. 131, 83-106.
    • (1986) Methods Enzymol , vol.131 , pp. 83-106
    • Creighton, T.E.1
  • 21
    • 33646350007 scopus 로고    scopus 로고
    • Folding of small disulfide-rich proteins: Clarifying the puzzle
    • Arolas, J. L., Aviles, F. X., Chang, J.-Y., and Ventura, S. (2006) Folding of small disulfide-rich proteins: Clarifying the puzzle, Trends Biochem. Sci. 31, 292-301.
    • (2006) Trends Biochem. Sci , vol.31 , pp. 292-301
    • Arolas, J.L.1    Aviles, F.X.2    Chang, J.-Y.3    Ventura, S.4
  • 23
    • 0026537987 scopus 로고
    • The disulfide folding pathway of BPTI
    • Creighton, T. E. (1992) The disulfide folding pathway of BPTI, Science 256, 111-114.
    • (1992) Science , vol.256 , pp. 111-114
    • Creighton, T.E.1
  • 24
    • 0026628991 scopus 로고
    • Native and non-native intermediates in the BPTI folding pathway
    • Goldenberg, D. P. (1992) Native and non-native intermediates in the BPTI folding pathway, Trends Biochem. Sci. 17, 257-261.
    • (1992) Trends Biochem. Sci , vol.17 , pp. 257-261
    • Goldenberg, D.P.1
  • 25
    • 0025949415 scopus 로고
    • Re-examination of the folding of BPTI: Predominance of native intermediates
    • Weissman, J. S., and Kim, P. S. (1991) Re-examination of the folding of BPTI: Predominance of native intermediates, Science 253, 1386-1393.
    • (1991) Science , vol.253 , pp. 1386-1393
    • Weissman, J.S.1    Kim, P.S.2
  • 26
    • 0029840319 scopus 로고    scopus 로고
    • The disulfide folding pathway of tick anticoagulant peptide, a kunitz-type inhibitor structurally homologous to BPTI
    • Chang, J.-Y. (1996) The disulfide folding pathway of tick anticoagulant peptide, a kunitz-type inhibitor structurally homologous to BPTI, Biochemistry 35, 11702-11709.
    • (1996) Biochemistry , vol.35 , pp. 11702-11709
    • Chang, J.-Y.1
  • 27
    • 0037646964 scopus 로고    scopus 로고
    • Major kinetic traps for the oxidative folding of leech carboxypeptidase inhibitor
    • Salamanca, S., Li, L., Vendrell, J., Aviles, F. X., and Chang, J.-Y. (2003) Major kinetic traps for the oxidative folding of leech carboxypeptidase inhibitor, Biochemistry 42, 6754-6761.
    • (2003) Biochemistry , vol.42 , pp. 6754-6761
    • Salamanca, S.1    Li, L.2    Vendrell, J.3    Aviles, F.X.4    Chang, J.-Y.5
  • 28
  • 29
    • 0035005366 scopus 로고    scopus 로고
    • Preorganized secondary structure as an important determinant of fast protein folding
    • Myers, J. K., and Oas, T. G. (2001) Preorganized secondary structure as an important determinant of fast protein folding, Nat. Struct. Biol. 8, 552-558.
    • (2001) Nat. Struct. Biol , vol.8 , pp. 552-558
    • Myers, J.K.1    Oas, T.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.