Residue solvent accessibilities in the unfolded polypeptide chain.
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.
Zielenkiewicz
P
P
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warszawa.
Saenger
W
W
D000595:Amino Acid Sequence; D001665:Binding Sites; D055592:Biophysical Phenomena; D001703:Biophysics; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry*; D017510:Protein Folding; D012997:Solvents; D013816:Thermodynamics
D009842:Oligopeptides; D012997:Solvents