Structural analysis and prediction of protein mutant stability using distance and torsion potentials: Role of secondary structure and solvent accessibility

Proteins: Structure, Function and Genetics

Volumn 66, Issue 1, 2007, Pages 41-52

  Parthiban, Vijaya ^a   Gromiha, M Michael ^b   Hoppe, Christian ^a   Schomburg, Dietmar ^a  

^a UNIVERSITY OF COLOGNE   (Germany)

^b NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

Author keywords

Point mutation; Protein stability prediction; Protein thermostability; Statistical potentials; Torsion angle potential

Indexed keywords

MUTANT PROTEIN;

ACCURACY; ARTICLE; CORRELATION ANALYSIS; MULTIPLE REGRESSION; POINT MUTATION; PREDICTION; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; RELIABILITY; STATISTICAL MODEL; STRUCTURE ANALYSIS; THERMOSTABILITY; VALIDATION PROCESS;

DATABASES, PROTEIN; MODELS, STATISTICAL; POINT MUTATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEINS; REGRESSION ANALYSIS; REPRODUCIBILITY OF RESULTS; SOLVENTS; THERMODYNAMICS;

EID: 33845664889     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21115     Document Type: Article

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