Solvent accessibility analysis on the mutants of Hsc70 ATPase fragment

Biophysical Chemistry

Volumn 71, Issue 2-3, 1998, Pages 99-111

  Kumarevel, T S ^a   Gromiha, M Michael ^b   Ponnuswamy, M N ^a  

^a UNIVERSITY OF MADRAS   (India)

^b INTERNATIONAL CENTRE FOR GENETIC ENGINEERING AND BIOTECHNOLOGY   (Italy)

Author keywords

Chaperone; Conformational stability; Free energy; HSC70; Hydrophobicity; Mutants; Solvent accessibility

Indexed keywords

ADENOSINE TRIPHOSPHATASE; HEAT SHOCK PROTEIN;

ARTICLE; ENERGY TRANSFER; ENZYME ACTIVE SITE; ENZYME ANALYSIS; HYDROPHOBICITY; MATHEMATICAL COMPUTING; MOLECULAR DYNAMICS; POINT MUTATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STABILITY;

HSP70 HEAT-SHOCK PROTEINS; PEPTIDE MAPPING; PEPTIDES; POINT MUTATION; PROTEIN CONFORMATION;

EID: 0032550148     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(97)00137-3     Document Type: Article

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