메뉴 건너뛰기




Volumn 23, Issue 10, 2010, Pages 769-780

A chemically modified α-amylase with a molten-globule state has entropically driven enhanced thermal stability

Author keywords

activation thermodynamics; calorimetry; entropy; enzyme kinetics; protein X ray crystallographic structure

Indexed keywords

ACTIVATION THERMODYNAMICS; BIOPHYSICAL PROPERTIES; CARBOXYL GROUPS; CHEMICALLY MODIFIED; HELICAL CONTENT; SECONDARY STRUCTURES; TERTIARY STRUCTURES; THERMAL STABILITY; THERMODYNAMIC ACTIVATION PARAMETERS; TRANSITION STATE; X RAY CRYSTAL STRUCTURES;

EID: 77956593720     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzq051     Document Type: Article
Times cited : (34)

References (68)
  • 7
    • 0028103275 scopus 로고
    • Collaborative Computational Project
    • Collaborative Computational Project. (1994) Acta Crystallogr. D Biol. Crystallogr., 50, 760-763.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 35
    • 0026475084 scopus 로고
    • Muller, N. (1992) TIBS, 17, 459-463.
    • (1992) TIBS , vol.17 , pp. 459-463
    • Muller, N.1
  • 40
    • 0029160445 scopus 로고
    • Ptitsyn, O.B. (1995) TIBS, 20, 376-379.
    • (1995) TIBS , vol.20 , pp. 376-379
    • Ptitsyn, O.B.1
  • 48


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.