Structure-based screening of binding affinities via small-angle X-ray scattering.

ABSTRACT: Protein-protein and protein-ligand interactions often involve conformational changes or structural rearrangements that can be quantified by solution small-angle X-ray scattering (SAXS). These scattering intensity measurements reveal structural details of the bound complex, the number of species involved and, additionally, the strength of interactions if carried out as a titration. Although a core part of structural biology workflows, SAXS-based titrations are not commonly used in drug discovery contexts. This is because prior knowledge of expected sample requirements, throughput and prediction accuracy is needed to develop reliable ligand screens. This study presents the use of the histidine-binding protein (26 kDa) and other periplasmic binding proteins to benchmark ligand screen performa

SUBMITTER: Chen PC 

PROVIDER: S-EPMC7340254 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature