Contribution of dipole-dipole interactions to the stability of the collagen triple helix.

ABSTRACT: Unveiling sequence-stability and structure-stability relationships is a major goal of protein chemistry and structural biology. Despite the enormous efforts devoted, answers to these issues remain elusive. In principle, collagen represents an ideal system for such investigations due to its simplified sequence and regular structure. However, the definition of the molecular basis of collagen triple helix stability has hitherto proved to be a difficult task. Particularly puzzling is the decoding of the mechanism of triple helix stabilization/destabilization induced by imino acids. Although the propensity-based model, which correlates the propensities of the individual imino acids with the structural requirements of the triple helix, is able to explicate most of the experimental data, it is un

SUBMITTER: Improta R 

PROVIDER: S-EPMC2327287 | biostudies-literature | 2008 May

REPOSITORIES: biostudies-literature