Exploration of Conformations for an Intrinsically Disordered Protein

Abstract

Intrinsically disordered proteins (IDP) are at the center of numerous biological processes, and attract consequently extreme interest in structural biology. A systematic enumeration of protein conformations, based on distance geometry, was performed on SERF1a, a 62-residue IDP involved in interactions with amyloid peptides. The results obtained with the interval Branch-and-Prune (iBP) approach haven been compared with those produced by flexible-meccano, using various predictions for backbone torsion angles ϕ and ψ, provided by TALOS and δ 2D. The similarity between profiles of local gyration radii provides to a certain extent a converged view of the SERF1a. A better convergence is observed when using the TALOS inputs than using the δ 2D inputs. flexible-meccano provides a less converged view of the protein conformational space than TAiBP.