Solvent accessible surface area of amino acid residues in globular proteins: Correlation of apparent transfer free energies with experimental hydrophobicity scales

Biomacromolecules

Volumn 10, Issue 5, 2009, Pages 1224-1237

  Shaytan, Alexey K ^a   Shaitan, Konstantin V ^a   Khokhlov, Alexei R ^a  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

Author keywords

[No Author keywords available]

Indexed keywords

ACID DISTRIBUTION; AMINO ACID RESIDUES; ENERGY SCALE; EVALUATION OF STABILITY; GLOBULAR PROTEINS; HYDROPHOBICITY SCALE; PROTEIN STRUCTURES; QUANTITATIVE STRUCTURE-ACTIVITY RELATIONSHIP STUDIES; RANDOM ENERGY MODELS; SOLVENT ACCESSIBLE SURFACE AREAS; STATISTICAL ENERGY; STATISTICAL SAMPLING;

AMINATION; AMINES; AMINO ACIDS; FREE ENERGY; HYDROPHOBICITY; ORGANIC SOLVENTS; PROTEINS; SAMPLING; SULFUR COMPOUNDS;

ORGANIC ACIDS;

AMINO ACID; GLOBULAR PROTEIN; ORGANIC SOLVENT; WATER;

APPARENT TRANSFER FREE ENERGY; ARTICLE; CORRELATION ANALYSIS; ENERGY; HYDROPHOBICITY; PARTITION COEFFICIENT; PRIORITY JOURNAL; PROTEIN STRUCTURE; SOLVENT EFFECT; SURFACE PROPERTY;

AMINO ACIDS; CYCLOHEXANES; DATABASES, PROTEIN; HYDROPHOBICITY; MODELS, STATISTICAL; OCTANOLS; PROTEINS; REPRODUCIBILITY OF RESULTS; SOLVENTS; SURFACE PROPERTIES; THERMODYNAMICS; WATER;

EID: 66149109184     PISSN: 15257797     EISSN: None     Source Type: Journal    
DOI: 10.1021/bm8015169     Document Type: Article

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