Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 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.

PubMed Disclaimer

References

    1. Proc Natl Acad Sci U S A. 1990 Feb 1;87(3):946-9 - PubMed
    1. J Mol Biol. 1984 Sep 5;178(1):63-89 - PubMed
    1. Annu Rev Biophys Bioeng. 1977;6:151-76 - PubMed
    1. Nature. 1975 Aug 28;256(5520):705-8 - PubMed
    1. Proteins. 1990;8(1):6-13 - PubMed

Publication types