Contribution of charged groups to the enthalpic stabilization of the folded states of globular proteins.

ABSTRACT: In this paper we use the results from all-atom molecular dynamics (MD) simulations of proteins and peptides to assess the individual contribution of charged atomic groups to the enthalpic stability of the native state of globular proteins and investigate how the distribution of charged atomic groups in terms of solvent accessibility relates to protein enthalpic stability. The contributions of charged groups is calculated using a comparison of nonbonded interaction energy terms from equilibrium simulations of charged amino acid dipeptides in water (the "unfolded state") and charged amino acids in globular proteins (the "folded state"). Contrary to expectation, the analysis shows that many buried, charged atomic groups contribute favorably to protein enthalpic stability. The strongest enthal

SUBMITTER: Dadarlat VM 

PROVIDER: S-EPMC4927099 | biostudies-literature | 2008 May

REPOSITORIES: biostudies-literature