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 language||English (US)|
|Number of pages||2|
|Journal||Journal of Physical Chemistry®|
|State||Published - 1995|
ASJC Scopus subject areas
- Physical and Theoretical Chemistry