Absolute hydration free energies of blocked amino acids: implications for protein solvation and stability.

ABSTRACT: Most proteins perform their function in aqueous solution. The interactions with water determine the stability of proteins and the desolvation costs of ligand binding or membrane insertion. However, because of experimental restrictions, absolute solvation free energies of proteins or amino acids are not available. Instead, solvation free energies are estimated based on side chain analog data. This approach implies that the contributions to free energy differences are additive, and it has often been employed for estimating folding or binding free energies. However, it is not clear how much the additivity assumption affects the reliability of the resulting data. Here, we use molecular dynamics-based free energy simulations to calculate absolute hydration free energies for 15 N-acetyl-methylam

SUBMITTER: Konig G 

PROVIDER: S-EPMC3552266 | biostudies-literature | 2013 Jan

REPOSITORIES: biostudies-literature