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Volumn 297, Issue 1, 2000, Pages 193-210

Thermal unfolding of an intermediate is associated with non-arrhenius kinetics in the folding of hen lysozyme

Author keywords

Circular dichroism; Folding intermediates; Hen egg white lysozyme; Mass spectrometry; Protein folding

Indexed keywords

LYSOZYME;

EID: 0034677664     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3540     Document Type: Article
Times cited : (65)

References (98)
  • 3
    • 0008112725 scopus 로고
    • Physical Chemistry, Oxford University Press, Oxford, UK
    • (1994) , pp. 927-959
    • Atkins, P.W.1
  • 12
    • 0000702636 scopus 로고
    • Absorption spectroscopy
    • Biophysical Chemistry (Part II)): Techniques for the Study of Biological Structure and Function, W.H. Freeman and Co., New York
    • (1980) , pp. 349-408
    • Cantor, C.R.1    Schimmel, P.R.2
  • 17
    • 0008111387 scopus 로고
    • Proteins, Structures and Molecular Properties, 2nd edit., W.H. Freeman and Co., New York
    • (1993) , pp. 309-328
    • Creighton, T.E.1
  • 30
    • 0027163998 scopus 로고
    • Protein folding and stability: The pathway of folding of barnase
    • (1993) FEBS Letters , vol.325 , pp. 5-16
    • Fersht, A.R.1
  • 32
    • 0008019725 scopus 로고    scopus 로고
    • Structure and Mechanism in Protein Sience-A Guide to Enzyme Catalysis and Protein Folding, W.H. Freeman and Co., New York
    • (1998) , pp. 54-59
    • Fersht, A.R.1
  • 33
    • 0030322627 scopus 로고    scopus 로고
    • Structure of very early protein folding intermediates: New insights through a variant of hydrogen exchange labelling
    • (1996) Fold. Design , vol.1 , pp. 407-417
    • Gladwin, S.T.1    Evans, P.A.2
  • 35
    • 0023041667 scopus 로고
    • Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: A comparative study of the folding reactions of α-lactalbumin and lysozyme
    • (1986) Biochemistry , vol.25 , pp. 6965-6972
    • Ikeguchi, M.1    Kuwajima, K.2    Mitani, M.3    Sugai, S.4
  • 38
    • 0026342150 scopus 로고
    • Folding of chymotrypsin inhibitor 2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding
    • (1991) Biochemistry , vol.30 , pp. 10436-10443
    • Jackson, S.E.1    Fersht, A.R.2
  • 43
    • 0008113343 scopus 로고
    • Protein dynamics: From the native to the unfolded state and back again
    • Modelling of Biomolecular Structures and Mechanisms (Pullman, A. et al., eds), Kluwer Academic, Dordrecht
    • (1995) , pp. 69-84
    • Karplus, M.1    Caflisch, A.2    Sali, A.3    Shakhnovich, E.4
  • 50
  • 51
    • 0031465967 scopus 로고    scopus 로고
    • 'New view' of protein folding reconciled with old through multiple unfolding simulations
    • (1997) Science , vol.278 , pp. 1928-1931
    • Lazaridis, T.1    Karplus, M.2
  • 53
    • 0029917969 scopus 로고    scopus 로고
    • The observed change in heat capacity accompanying the thermal unfolding of proteins depends on the composition of the solution and on the method employed to change the temperature of unfolding
    • (1996) Biochemistry , vol.35 , pp. 3059-3062
    • Liu, Y.1    Sturtevant, J.M.2
  • 77
    • 0030961780 scopus 로고    scopus 로고
    • The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions
    • (1997) Nature Struct. Biol. , vol.4 , pp. 298-304
    • Raschke, T.M.1    Marqusee, S.2
  • 84
    • 0021525532 scopus 로고
    • Characterization of the transition state of lysozyme unfolding. I. Effect of protein-solvent interactions on the transition state
    • (1984) Biopolymers , vol.23 , pp. 2473-2488
    • Segawa, S.I.1    Sugihara, M.2
  • 89
    • 85012750408 scopus 로고
    • Kinetic characterization of complex reaction systems
    • Comprehensive Chemical Kinetics (Bamford, C. H. and Tipper, C. F. H., eds), Elsevier, Amsterdam
    • (1969) , pp. 1-80
    • Szabo, A.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.