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Hydrophobic regions on protein surfaces. Derivation of the solvation energy from their area distribution in crystallographic protein structures
Author(s) -
Eisenhaber Frank
Publication year - 1996
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560050821
Subject(s) - solvation , macromolecule , chemistry , solvation shell , accessible surface area , implicit solvation , surface energy , crystallography , hydrophobic effect , chemical physics , thermodynamics , surface (topology) , computational chemistry , solvent , geometry , organic chemistry , physics , biochemistry , mathematics
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‐Å 2 ), with a statistical uncertainty of ±2 cal/(mol‐Å 2 ) 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.