Biophysical Journal 63: 1483-1486 (1992)
© 1992 the Biophysical Society

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Residue solvent accessibilities in the unfolded polypeptide chain.

Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warszawa.

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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