Peptide conformations are restricted by solution stability

John S. Perkyns, Bernard Pettitt

Research output: Contribution to journalArticle

6 Scopus citations

Abstract

Thermodynamic stability and statistical mechanical theory are applied to a model of a zwitterionic tripeptide of sequence Gly-Ala-Gly in high-concentration NaCl solution. It is found that many peptide conformations cannot exist in equilibrium with the salt-water solvent as a single liquid phase. This suggests a single explanation for salting proteins into and out of solution, unique biologically active protein structures, and small energy differences between denatured and folded states, while also implying a mechanism for the resolution to the Levinthal paradox.

Original languageEnglish (US)
Pages (from-to)1-2
Number of pages2
JournalJournal of Physical Chemistry®
Volume99
Issue number1
StatePublished - 1995
Externally publishedYes

    Fingerprint

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry

Cite this