Linear free-energy model description of the conformational stability of uracil-DNA glycosylase inhibitor. A thermodynamic characterization of interaction with denaturant and cold denaturation

European Journal of Biochemistry

Volumn 261, Issue 3, 1999, Pages 610-617

  Reddy, G Bhanuprakash ^a   Purnapatre, Kedar ^a   Lawrence, Rajendran ^a   Roy, Sudipta ^a   Varshney, Umesh ^a   Surolia, Avadhesha ^a  

^a INDIAN INSTITUTE OF SCIENCE   (India)

Author keywords

Cold denaturation; Heat capacity change; Linear free energy model; Protein stability; Uracil DNA glycosylase inhibitor

Indexed keywords

ENZYME INHIBITOR; GUANIDINE; MONOMER; URACIL DNA GLYCOSYLTRANSFERASE;

ARTICLE; BACILLUS SUBTILIS; BACTERIOPHAGE; ENTHALPY; ENTROPY; HEAT EXCHANGE; HYDROPHOBICITY; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN STABILITY; THERMODYNAMICS;

COLD; DNA GLYCOSYLASES; ENZYME INHIBITORS; ESCHERICHIA COLI; GUANIDINE; MODELS, CHEMICAL; N-GLYCOSYL HYDROLASES; PROTEIN CONFORMATION; PROTEIN DENATURATION; THERMODYNAMICS; URACIL-DNA GLYCOSIDASE;

EID: 0033136052     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00271.x     Document Type: Article

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