Thermodynamic and Stereochemical Parameters to Evaluate Stability of
Hydrophobic Cores of Globular Proteins
A. V. Trikulenko
Franko Lvov State University, ul. Grushevskogo 4, Lvov, 290005 Ukraine;
fax: (0322) 27-1668
Received January 28, 1998; Revision received July 7, 1998
This work presents a hydrophobicity scale of nonpolar amino acids
calculated by the method of Tanford. The evaluation of stability of
hydrophobic cores of globular proteins using this hydrophobicity scale
is described. Stereochemical and thermodynamic parameters are presented
that make it possible to choose replacements for side chains of
nonpolar amino acid residues in the hydrophobic cores in order to
increase their stability.
KEY WORDS: hydrophobicity scale, replacement of nonpolar amino
acid residues, stability of hydrophobic cores