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Volumn 70, Issue 6, 2000, Pages 699-703

Trehalose delays the reversible but not the irreversible thermal denaturation of cutinase

Author keywords

Cutinase; Irreversible inactivation; Thermal unfolding; Trehalose

Indexed keywords

ACTIVATION ENERGY; ENZYME KINETICS; PH EFFECTS; RATE CONSTANTS; THERMAL EFFECTS; THERMODYNAMIC STABILITY;

EID: 0034694819     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/1097-0290(20001220)70:6<699::AID-BIT13>3.0.CO;2-N     Document Type: Article
Times cited : (40)

References (17)
  • 4
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    • Klibanov, A.M.1    Ahern, T.J.2
  • 9
    • 0002846347 scopus 로고    scopus 로고
    • Measuring the conformational stability of a protein
    • Creighton TE, editor. Protein structure: a practical approach. Oxford: IRL Press
    • (1997) , pp. 299-321
    • Pace, C.N.1    Sholtz, J.M.2
  • 12
    • 0029198906 scopus 로고
    • Solvent stabilization of protein structure
    • Shirley BA, editor. Protein stability and folding: Theory and practice. Totowa, NJ: Humana Press
    • (1995) , pp. 253-269
    • Timasheff, S.N.1
  • 13
    • 0002643399 scopus 로고
    • Minimizing protein inactivation
    • Creighton TE, editor. Protein function: a practical approach. Oxford: IRL Press
    • (1989) , pp. 213-218
    • Volkin, D.B.1    Klibanov, A.M.2
  • 15
    • 0031013887 scopus 로고    scopus 로고
    • Mechanisms of the stabilization of ribonuclease A by sorbitol: Preferential hydration is greater for the denaturated than for the native protein
    • (1997) Protein Sci , vol.6 , pp. 211-221
    • Xie, G.1    Timasheff, S.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.