Gas-Phase Unfolding of Protein Complexes Distinguishes Conformational Isomers.

ABSTRACT: Proteins can adopt different conformational states that are important for their biological function and, in some cases, can be responsible for their dysfunction. The essential roles that proteins play in biological systems make distinguishing the structural differences between these conformational states both fundamentally and practically important. Here, we demonstrate that collision-induced unfolding (CIU), in combination with ion mobility-mass spectrometry (IM-MS) measurements, distinguish subtly different conformational states for protein complexes. Using the open and closed states of the β-lactoglobulin (βLG) dimer as a model, we show that these two conformational isomers unfold during collisional activation to generate distinct states that are readily separated by IM-MS. Extensive mo

SUBMITTER: Nash S 

PROVIDER: S-EPMC9771597 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature