메뉴 건너뛰기




Volumn 363, Issue 1827, 2005, Pages 565-573

Kinetic equivalence of the heat and cold structural transitions of λ6-85

Author keywords

Cold denaturation; Heat denaturation; Kinetics; Phase transition; Pressure denaturation; Temperature jump

Indexed keywords


EID: 12944261949     PISSN: 1364503X     EISSN: None     Source Type: Journal    
DOI: 10.1098/rsta.2004.1508     Document Type: Article
Times cited : (9)

References (22)
  • 1
    • 0001261542 scopus 로고    scopus 로고
    • A single-sweep, nanosecond time resolution laser temperature-jump apparatus
    • Ballew, R. M., Sabelko, J., Reiner, C. & Gruebele, M. 1996 A single-sweep, nanosecond time resolution laser temperature-jump apparatus. Rev. Scient. Instrum. 67, 3694-3699.
    • (1996) Rev. Scient. Instrum. , vol.67 , pp. 3694-3699
    • Ballew, R.M.1    Sabelko, J.2    Reiner, C.3    Gruebele, M.4
  • 2
    • 0031005061 scopus 로고    scopus 로고
    • The energy landscape of a fast-folding protein mapped by Ala → Gly substitutions
    • Burton, R. E., Huang, G. S., Daugherty, M. A., Calderone, T. L. & Oas, T. G. 1997 The energy landscape of a fast-folding protein mapped by Ala → Gly substitutions. Nat. Struct. Biol. 4, 305-310.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 305-310
    • Burton, R.E.1    Huang, G.S.2    Daugherty, M.A.3    Calderone, T.L.4    Oas, T.G.5
  • 4
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch, H. 1967 Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6, 1948-1954.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 5
    • 0033996482 scopus 로고    scopus 로고
    • Submicrosecond real-time fluorescence detection: Application to protein folding
    • Ervin, J., Sabelko, J. & Gruebele, M. 2000 Submicrosecond real-time fluorescence detection: application to protein folding. J. Photochem. Photobiol. B 54, 1-15.
    • (2000) J. Photochem. Photobiol. B , vol.54 , pp. 1-15
    • Ervin, J.1    Sabelko, J.2    Gruebele, M.3
  • 6
    • 0036286323 scopus 로고    scopus 로고
    • What causes hyperfluorescence: Folding intermediates or conformationally flexible native states?
    • Ervin, J., Larios, E., Osvath, S., Schulten, K. & Gruebele, M. 2002 What causes hyperfluorescence: folding intermediates or conformationally flexible native states? Biophys. J. 83, 473-483.
    • (2002) Biophys. J. , vol.83 , pp. 473-483
    • Ervin, J.1    Larios, E.2    Osvath, S.3    Schulten, K.4    Gruebele, M.5
  • 8
    • 0015236387 scopus 로고
    • Reversible pressure-temperature unfolding of chymotrypsinogen
    • Hawley, S. A. 1971 Reversible pressure-temperature unfolding of chymotrypsinogen. Biochemistry 10, 2436-2442.
    • (1971) Biochemistry , vol.10 , pp. 2436-2442
    • Hawley, S.A.1
  • 10
    • 0029934661 scopus 로고    scopus 로고
    • Heat and cold denatured states of monomeric a repressor are thermodynamically and conformationally equivalent
    • Huang, G. S. & Oas, T. G. 1996 Heat and cold denatured states of monomeric A repressor are thermodynamically and conformationally equivalent. Biochemistry 35, 6173-6180.
    • (1996) Biochemistry , vol.35 , pp. 6173-6180
    • Huang, G.S.1    Oas, T.G.2
  • 11
    • 0030582432 scopus 로고    scopus 로고
    • Hydrogen-exchange kinetics in the cold denatured state of ribonuclease a
    • Nash, D., Lee, B. & Jonas, J. 1996 Hydrogen-exchange kinetics in the cold denatured state of ribonuclease A. Biochim. Biophys. Acta 1297, 40-48.
    • (1996) Biochim. Biophys. Acta , vol.1297 , pp. 40-48
    • Nash, D.1    Lee, B.2    Jonas, J.3
  • 14
    • 0016224361 scopus 로고
    • A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study
    • Privalov, P. L. &: Khechinashvili, N. N. 1974 A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study. J. Mol. Biol. 86, 665-684.
    • (1974) J. Mol. Biol. , vol.86 , pp. 665-684
    • Privalov, P.L.1    Khechinashvili, N.N.2
  • 15
    • 0015143060 scopus 로고
    • Thermodynamic analysis of thermal transitions in globular proteins. I. Calorimetric study of ribotrypsinogen, ribonuclease and myoglobin
    • Privalov, P. L., Khechinashvili, N. N. & Atanasov, B. P. 1971 Thermodynamic analysis of thermal transitions in globular proteins. I. Calorimetric study of ribotrypsinogen, ribonuclease and myoglobin. Biopolymers 10, 1865-1890.
    • (1971) Biopolymers , vol.10 , pp. 1865-1890
    • Privalov, P.L.1    Khechinashvili, N.N.2    Atanasov, B.P.3
  • 16
    • 0037171140 scopus 로고    scopus 로고
    • Revisiting volume changes in pressure-induced protein unfolding
    • Royer, C. A. 2002 Revisiting volume changes in pressure-induced protein unfolding. Biochim. Biophys. Acta 1595, 201-209.
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 201-209
    • Royer, C.A.1
  • 17
    • 0000864144 scopus 로고    scopus 로고
    • The cold denatured ensemble of apomyoglobin: Implications for the early steps of folding
    • Sabelko, J., Ervin, J. & Gruebele, M. 1998 The cold denatured ensemble of apomyoglobin: implications for the early steps of folding. J. Phys. Chem. B 102, 1806-1819.
    • (1998) J. Phys. Chem. B , vol.102 , pp. 1806-1819
    • Sabelko, J.1    Ervin, J.2    Gruebele, M.3
  • 18
    • 0032989351 scopus 로고    scopus 로고
    • Observation of strange kinetics in protein folding
    • Sabelko, J., Ervin, J. & Gruebele, M. 1999 Observation of strange kinetics in protein folding. Proc. Natl Acad. Sci. USA 96, 6031-6036.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 6031-6036
    • Sabelko, J.1    Ervin, J.2    Gruebele, M.3
  • 19
    • 5444232650 scopus 로고    scopus 로고
    • Drying-induced hydrophobic polymer collapse
    • ten Wolde, P. R. & Chandler, D. 2002 Drying-induced hydrophobic polymer collapse. J. Mol. Biol. 311, 373-393.
    • (2002) J. Mol. Biol. , vol.311 , pp. 373-393
    • Wolde, P.R.1    Chandler, D.2
  • 20
    • 0038329308 scopus 로고    scopus 로고
    • Folding at the speed limit
    • Yang, W. Y. & Gruebele, M. 2003 Folding at the speed limit. Nature 423, 193-197.
    • (2003) Nature , vol.423 , pp. 193-197
    • Yang, W.Y.1    Gruebele, M.2
  • 21
    • 3042814557 scopus 로고    scopus 로고
    • Folding lambda repressor at its speed limit
    • Yang, W. Y. & Gruebele, M. 2004a Folding lambda repressor at its speed limit. Biophys. J. 87, 596-608.
    • (2004) Biophys. J. , vol.87 , pp. 596-608
    • Yang, W.Y.1    Gruebele, M.2
  • 22
    • 5444267817 scopus 로고    scopus 로고
    • Rate-temperature relationships in lambda repressor fragment 6 85 folding
    • Yang, W. Y. & Gruebele, M. 2004b Rate-temperature relationships in lambda repressor fragment 6 85 folding. Biochemistry 43, 13 018-13 025.
    • (2004) Biochemistry , vol.43 , pp. 13018-13025
    • Yang, W.Y.1    Gruebele, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.