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Volumn 39, Issue 40, 2000, Pages 12365-12374

Thermodynamic and structural studies of cavity formation in proteins suggest that loss of packing interactions rather than the hydrophobic effect dominates the observed energetics

(2) Ratnaparkhi, G S a,b Varadarajan, R a,c

a INDIAN INSTITUTE OF SCIENCE (India)

b TATA INSTITUTE OF FUNDAMENTAL RESEARCH (India)

c JAWAHARLAL NEHRU CENTRE FOR ADVANCED SCIENTIFIC RESEARCH (India)

Author keywords

[No Author keywords available]

Indexed keywords

MUTANT PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; CRYSTALLIZATION; ENERGY TRANSFER; ENTHALPY; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN INTERACTION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; THERMODYNAMICS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BACTERIOPHAGE T4; CRYSTALLOGRAPHY, X-RAY; HUMANS; MOLECULAR SEQUENCE DATA; MURAMIDASE; PEPTIDE FRAGMENTS; PHENYLALANINE; POINT MUTATION; PROTEIN BINDING; PROTEIN FOLDING; RIBONUCLEASES; STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS; WATER;

EID: 0034633945 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi000775k Document Type: Article

Times cited : (69)

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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.