Thermodynamic analysis of interactions between denaturants and protein surface exposed on unfolding: Interpretation of urea and guanidinium chloride m-values and their correlation with changes in accessible surface area (ASA) using preferential interaction coefficients and the local-bulk domain model

Proteins: Structure, Function and Genetics

Volumn 41, Issue SUPPL. 4, 2000, Pages 72-85

  Kozlov, Alexander G ^a   Lohman, Timothy M ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Activity coefficient; Linear extrapolation model; Partition coefficient; Peptide backbone; Protein stability

Indexed keywords

AMIDE; CATION; DISULFIDE; GUANIDINE; OLIGOPEPTIDE; PROTEIN; UREA;

ARTICLE; CALCULATION; CONCENTRATION RESPONSE; ENERGY; MATHEMATICAL MODEL; PARTITION COEFFICIENT; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; QUANTITATIVE ASSAY; THERMODYNAMICS; CHEMICAL MODEL; CHEMISTRY; PROTEIN DENATURATION;

GUANIDINE; MODELS, CHEMICAL; PROTEIN DENATURATION; PROTEINS; THERMODYNAMICS; UREA;

EID: 0033772098     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/1097-0134(2000)41:4+<72::AID-PROT70>3.0.CO;2-7     Document Type: Article

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