Exploration of conformations for an IDP

Shu-Yu Huang (1) , Chi-Fon Chang (1) , Jung-Hsin Lin (1) , Thérèse Malliavin (2)

1 Academia Sinica
2 LPCT - Laboratoire de Physique et Chimie Théoriques

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 threading-adapted interval Branch-and-Prune (TAiBP) approach haven been analyzed using various input predictions for backbone torsion angles ϕ and ψ, provided by TALOS and δ2D, as well as a NOE measurement. The fitting of SAXS data permitted to select various sets of conformations depending on the input predictions The similarity between profiles of local gyration radii provides to a certain extent a converged view of the SERF1a. A better convergence of these profiles is observed when using the TALOS inputs than using the δ2D inputs. All sets of conformations point to the same locations for maxima of pocketedness along protein sequences.

Mots clés: Solution-state NMR; Disordered protein; Distance Geometry

Domaines: Sciences du Vivant [q-bio]; Informatique [cs]

Shu-Yu Huang, Chi-Fon Chang, Jung-Hsin Lin, Thérèse Malliavin. Exploration of conformations for an IDP. The 27th Biophysics Conference, May 2023, Hualien, Taiwan. ⟨hal-04545891⟩