Thermodynamics of Conformational Transitions in a Disordered Protein Backbone Model.

ABSTRACT: Conformational entropy is expected to contribute significantly to the thermodynamics of structural transitions in intrinsically disordered proteins or regions in response to protein/ligand binding, posttranslational modifications, and environmental changes. We calculated the backbone (dihedral) conformational entropy of oligoglycine (Gly_N), a protein backbone mimic and model intrinsically disordered region, as a function of chain length (N=3, 4, 5, 10, and 15) from simulations using three different approaches. The backbone conformational entropy scales linearly with chain length with a slope consistent with the entropy of folding of well-structured proteins. The entropic contributions of second-order dihedral correlations are predominantly through intraresidue ϕ-ψ pairs, suggest

SUBMITTER: Drake JA 

PROVIDER: S-EPMC6026333 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature