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. 1992 Dec;63(6):1483-6.
doi: 10.1016/S0006-3495(92)81746-0.

Residue solvent accessibilities in the unfolded polypeptide chain

P Zielenkiewicz  1 , W Saenger
Affiliations

Residue solvent accessibilities in the unfolded polypeptide chain

P Zielenkiewicz et al. Biophys J. 1992 Dec.

Abstract

The difference of solvent accessibilities in the native and unfolded states of the protein is used as a measure of the hydrophobic contribution to the free energy of folding. We present a new approximation of amino acids solvent accessibilities in the unfolded state based on the 1-ns molecular dynamics simulation of Ala-X-Ala tripeptides at a temperature of 368 K. The standard accessibility values averaged from the molecular dynamics study are significantly lower from those previously obtained by considering only selected conformations of Ala-X-Ala tripeptides.

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