title: Role of hydrophobicity in protein structure is overestimated.
abstract: Some microcalorimetrically measured and theoretically calculated thermodynamic interaction coefficients of amino acid compounds in aqueous and peptidic systems have been collected, and are reported here. They indicate that although hydrophobicity contributes to the stability of the native structure of proteins, its influence on their exact configuration is limited.
authors.affiliation: Dept. of Chemistry, Free University, Amsterdam, The Netherlands.
authors.forename: M
authors.initials: M
authors.lastname: Bloemendal
authors.forename: Y
authors.initials: Y
authors.lastname: Marcus
authors.forename: A H
authors.initials: AH
authors.lastname: Sijpkes
authors.forename: G
authors.initials: G
authors.lastname: Somsen
mesh_terms: D011487:Protein Conformation; D012997:Solvents; D013816:Thermodynamics; D014867:Water
chemical_list: D012997:Solvents; D014867:Water