Thermodynamic and stereochemical parameters to evaluate stability of hydrophobic cores of globular proteins.
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.
Trikulenko
A V
AV
Franko Lvov State University, Lvov, 290005, Ukraine.
D000596:Amino Acids / Q000737:chemistry*; D002151:Calorimetry; D002918:Chymotrypsin / Q000737:chemistry; D015786:Cytochromes b5 / Q000737:chemistry; D009211:Myoglobin / Q000737:chemistry; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012260:Ribonucleases / Q000737:chemistry; D013816:Thermodynamics
D000596:Amino Acids; D009211:Myoglobin; D011506:Proteins; D015786:Cytochromes b5; D012260:Ribonucleases; D002918:Chymotrypsin