Using modern approaches to sedimentation velocity to detect conformational changes in proteins.

ABSTRACT: It has been known for decades that proteins undergo conformational changes in response to binding ligands. Such changes are usually accompanied by a loss of entropy by the protein, and thus conformational changes are integral to the thermodynamics of ligand association. Methods to detect these alterations are numerous; here, we focus on the sedimentation velocity (SV) mode of AUC, which has several advantages, including ease of use and rigorous data-selection criteria. In SV, it is assumed that conformational changes manifest primarily as differences in the sedimentation coefficient (the s-value). Two methods of determining s-value differences were assessed. The first method used the widely adopted c(s) distribution to gather statistics on the s-value differences to determine whether the o

SUBMITTER: Brautigam CA 

PROVIDER: S-EPMC7704540 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature