Forecasting the upper bound free energy difference between protein native-like structures

Abstract

Using a combination of statistical thermodynamics and the Gershgorin theorem we computed, in the thermodynamic limit, a plausible value for the upper bound of the free energy difference between native-like structures of monomeric globular proteins. The validity of our result is discussed herein in terms of both the observed free-energy change between the native and denatured states and the micro stability free-energy values obtained from the observed micro-unfolding tendency of nine monomeric globular proteins.