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- W2003264173 endingPage "1686" @default.
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- W2003264173 abstract "For the first time, a direct approach for the derivation of an atomic solvation parameter from macromolecular structural data alone is presented. The specific free energy of solvation for hydrophobic surface regions of proteins is delineated from the area distribution of hydrophobic surface patches. The resulting value is 18 cal/(mol.A2), with a statistical uncertainty of +/-2 cal/mol.A2) at the 5% significance level. It compares favorably with the parameters for carbon obtained by other authors who use the the crystal geometry of succinic acid or energies of transfer from hydrophobic solvent to water for small organic compounds. Thus, the transferability of atomic solvation parameters for hydrophobic atoms to macromolecules has been directly demonstrated. A careful statistical analysis demonstrates that surface energy parameters derived from thermodynamic data of protein mutation experiments are clearly less confident." @default.
- W2003264173 created "2016-06-24" @default.
- W2003264173 creator A5007579711 @default.
- W2003264173 date "1996-08-01" @default.
- W2003264173 modified "2023-10-02" @default.
- W2003264173 title "Hydrophobic regions on protein surfaces. Derivation of the solvation energy from their area distribution in crystallographic protein structures" @default.
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- W2003264173 doi "https://doi.org/10.1002/pro.5560050821" @default.
- W2003264173 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2143472" @default.
- W2003264173 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8844856" @default.
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