Stability analysis for the cavity-filling mutations of the Myb DNA- binding domain utilizing free-energy calculations

Proteins: Structure, Function and Genetics

Volumn 38, Issue 2, 2000, Pages 197-209

  Kono, Hidetoshi ^a,c   Saito, Minoru ^b   Sarai, Akinori ^a  

^a RIKEN TSUKUBA INSTITUTE   (Japan)

^b HIROSAKI UNIVERSITY   (Japan)

^c UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

Cavity filling mutation; Free energy perturbation; Molecular dynamics; Nonnatural amino acid; Thermodynamic stability

Indexed keywords

ARTICLE; COVALENT BOND; DNA BINDING; ENTHALPY; ENTROPY; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN STABILITY; SITE DIRECTED MUTAGENESIS; THERMODYNAMICS; TRANSCRIPTION REGULATION;

AMINO ACID SUBSTITUTION; BINDING SITES; DNA; ISOLEUCINE; LEUCINE; MODELS, MOLECULAR; MUTATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTO-ONCOGENE PROTEINS C-MYB; THERMODYNAMICS; VALINE;

EID: 0034142174     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(20000201)38:2<197::AID-PROT8>3.0.CO;2-B     Document Type: Article

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