Revisiting "reverse hydrophobic effect": Applicable only to coil mutations at the surface

Biopolymers

Volumn 91, Issue 7, 2009, Pages 591-599

  Gromiha, M Michael ^a  

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

Author keywords

Free energy change; Hydrophobicity; Mutants; Nonnative interactions; Protein stability

Indexed keywords

AMINO ACID SUBSTITUTION; CONFORMATIONAL PROPERTIES; FREE ENERGY CHANGE; HYDROPHOBIC EFFECT; MUTANTS; NONNATIVE INTERACTIONS; PROTEIN STABILITY; PROTEIN STRUCTURES; SECONDARY STRUCTURES; SIDE-CHAIN; SOLVENT ACCESSIBILITY; NON-NATIVE INTERACTIONS;

AMINES; AMINO ACIDS; FREE ENERGY; HYDROPHOBICITY; ORGANIC ACIDS; STRUCTURAL ANALYSIS; PROTEINS;

STABILITY;

AMINO ACID; MUTANT PROTEIN; LYSOZYME;

AMINO ACID SUBSTITUTION; ARTICLE; ENTROPY; HYDROPHOBICITY; MUTATIONAL ANALYSIS; PROTEIN CONFORMATION; PROTEIN DETERMINATION; PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; STRUCTURE ANALYSIS; SURFACE PROPERTY; CONTROLLED STUDY; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; THERMODYNAMICS; AMINO ACID SEQUENCE; CHEMISTRY; GENETICS; HUMAN; METABOLISM; MOLECULAR GENETICS; MUTATION; PROTEIN FOLDING;

AMINO ACID SEQUENCE; AMINO ACIDS; HUMANS; HYDROPHOBICITY; MOLECULAR SEQUENCE DATA; MURAMIDASE; MUTANT PROTEINS; MUTATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; THERMODYNAMICS;

EID: 68349156292     PISSN: 00063525     EISSN: 10970282     Source Type: Journal    
DOI: 10.1002/bip.21187     Document Type: Article

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