Refining conformational ensembles of flexible proteins against small-angle x-ray scattering data.

ABSTRACT: Intrinsically disordered proteins and flexible regions in multidomain proteins display substantial conformational heterogeneity. Characterizing the conformational ensembles of these proteins in solution typically requires combining one or more biophysical techniques with computational modeling or simulations. Experimental data can either be used to assess the accuracy of a computational model or to refine the computational model to get a better agreement with the experimental data. In both cases, one generally needs a so-called forward model (i.e., an algorithm to calculate experimental observables from individual conformations or ensembles). In many cases, this involves one or more parameters that need to be set, and it is not always trivial to determine the optimal values or to understan

SUBMITTER: Pesce F 

PROVIDER: S-EPMC8633713 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature