Correlating hydration shell structure with amino acid hydrophobicity

Autor:	Lema Tadesse, Lee R. Walters, David Hecht
Rok vydání:	1993
Předmět:	chemistry.chemical_classification Aqueous solution Stereochemistry Hydrogen bond General Chemistry Biochemistry Catalysis Amino acid Accessible surface area Solvent Crystallography Colloid and Surface Chemistry Solvation shell chemistry Molecule Hydrophobicity scales
Zdroj:	Journal of the American Chemical Society. 115:3336-3337
ISSN:	1520-5126 0002-7863
DOI:	10.1021/ja00061a045
Popis:	the degree of solvent-solvent hydrogen bonding in the hydration shells surrounding eight "hydrophobic" amino acids. These structural data are correlated with ther- modynamic criteria for amino acid hydrophobicity. Hydrophobicity has traditionally been defined in classical thermodynamic terms that are based upon macroscopic properties of solutes and their solutions. These include (a) the free energy of transfer of compounds from a nonaqueous to an aqueous pha~el-~
Databáze:	OpenAIRE
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