Conformational entropy of alanine versus glycine in protein denatured states.

ABSTRACT: The presence of a solvent-exposed alanine residue stabilizes a helix by 0.4-2 kcal.mol(-1) relative to glycine. Various factors have been suggested to account for the differences in helical propensity, from the higher conformational freedom of glycine sequences in the unfolded state to hydrophobic and van der Waals' stabilization of the alanine side chain in the helical state. We have performed all-atom molecular dynamics simulations with explicit solvent and exhaustive sampling of model peptides to address the backbone conformational entropy difference between Ala and Gly in the denatured state. The mutation of Ala to Gly leads to an increase in conformational entropy equivalent to approximately 0.4 kcal.mol(-1) in a fully flexible denatured, that is, unfolded, state. But, this energy is

SUBMITTER: Scott KA 

PROVIDER: S-EPMC1815238 | biostudies-literature | 2007 Feb

REPOSITORIES: biostudies-literature