Sequence Effects on Size, Shape, and Structural Heterogeneity in Intrinsically Disordered Proteins.

ABSTRACT: Intrinsically disordered proteins (IDPs) lack well-defined three-dimensional structures, thus challenging the archetypal notion of structure-function relationships. Determining the ensemble of conformations that IDPs explore under physiological conditions is the first step toward understanding their diverse cellular functions. Here, we quantitatively characterize the structural features of IDPs as a function of sequence and length using coarse-grained simulations. For diverse IDP sequences, with the number of residues ( N_T) ranging from 20 to 441, our simulations not only reproduce the radii of gyration ( R_g) obtained from experiments, but also predict the full scattering intensity profiles in excellent agreement with small-angle X-ray scattering experiments. The R

SUBMITTER: Baul U 

PROVIDER: S-EPMC6920032 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature