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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