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Volumn 96, Issue 2-3, 2002, Pages 109-116

The heat capacity paradox of ligand binding proteins: Reconciling the microscopic and macroscopic world

Author keywords

Calorimetry; Grand canonic; Ligand binding; Partition function; Statistical thermodynamics

Indexed keywords

LIGAND; M PROTEIN; PROTEIN;

EID: 0037007463     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(02)00016-9     Document Type: Article
Times cited : (6)

References (17)
  • 8
    • 0026734102 scopus 로고
    • Two-dimensional differential scanning calorimetry: Simultaneous resolution of intrinsic protein structural energetics and ligand binding interactions by global linkage analysis
    • (1992) Anal. Biochem. , vol.203 , pp. 259-268
    • Straume, M.1    Freire, E.2
  • 10
    • 84996119574 scopus 로고
    • Determination of thermodynamic functions from scanning calorimetry data. II. For the system that includes self-dissociation/association processes
    • (1988) Biopolymers , vol.27 , pp. 271-297
    • Kidokoro, S.-I.1    Uedaira, H.2    Wada, A.3
  • 11
    • 0000103534 scopus 로고
    • Statistical thermodynamic analysis of the heat capacity function associated with protein folding-unfolding transitions
    • (1989) Comments Mol. Cell. Biophys. , vol.6 , pp. 123-140
    • Freire, E.1
  • 16


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.