Dissection of Factors Affecting the Variability of the Peptide Bond Geometry and Planarity.

ABSTRACT: Proteins frequently assume complex three-dimensional structures characterized by marginal thermodynamic stabilities. In this scenario, deciphering the folding code of these molecular giants with clay feet is a cumbersome task. Studies performed in last years have shown that the interplay between backbone geometry and local conformation has an important impact on protein structures. Although the variability of several geometrical parameters of protein backbone has been established, the role of the structural context in determining these effects has been hitherto limited to the valence bond angle τ (NC ^α C). We here investigated the impact of different factors on the observed variability of backbone geometry and peptide bond planarity. These analyses corroborate the

SUBMITTER: Balasco N 

PROVIDER: S-EPMC5661080 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature