Relative importance of secondary structure and solvent accessibility to the stability of protein mutants.: A case study with amino acid properties and energetics on T4 and human lysozymes

Computational Biology and Chemistry

Volumn 29, Issue 1, 2005, Pages 25-35

  Saraboji, K ^a   Gromiha, M Michael ^b   Ponnuswamy, M N ^a  

^a UNIVERSITY OF MADRAS   (India)

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

Author keywords

Amino acid properties; Free energy; Multiple regression analysis; Protein mutants; Protein stability

Indexed keywords

AMINO ACIDS; ELECTROSTATICS; ENZYME INHIBITION; FREE ENERGY; HYDROGEN BONDS; HYDROPHOBICITY; MATHEMATICAL MODELS; PROTEINS; REGRESSION ANALYSIS; THERMODYNAMIC STABILITY;

AMINO ACID PROPERTIES; MULTIPLE REGRESSION ANALYSIS; PROTEIN MUTANTS; PROTEIN STABILITY;

MUTAGENESIS;

AMINO ACID; LYSOZYME; SOLVENT;

ARTICLE; BACTERIOPHAGE T4; CHEMISTRY; ENZYMOLOGY; GENETICS; GENOMIC INSTABILITY; HUMAN; HYDROPHOBICITY; MUTATION; PH; PROTEIN DATABASE; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; THERMODYNAMICS;

AMINO ACIDS; BACTERIOPHAGE T4; DATABASES, PROTEIN; GENOMIC INSTABILITY; HUMANS; HYDROGEN-ION CONCENTRATION; HYDROPHOBICITY; MURAMIDASE; MUTATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SOLVENTS; THERMODYNAMICS;

EID: 12444274892     PISSN: 14769271     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.compbiolchem.2004.12.002     Document Type: Article

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