Estimates of the loss of main-chain conformational entropy of different residues on protein folding.
The average contribution of conformational entropy for individual amino acid residues towards the free energy of protein folding is not well understood. We have developed empirical scales for the loss of the main-chain (torsion angles, phi and psi) conformational entropy by taking its side-chain into account. The analysis shows that the main-chain component of the total conformational entropy loss for a residue is significant and reflects intrinsic characteristics associated with individual residues. The values have direct correlation with the hydrophobicity values and this has important bearing on the folding process. Proteins 1999;36:332-339.
Department of Biochemistry, Bose Institute, Calcutta, India.
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D019943:Amino Acid Substitution; D000596:Amino Acids / Q000737:chemistry; D018360:Crystallography, X-Ray; D008956:Models, Chemical; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
D000596:Amino Acids; D011506:Proteins