Single molecule mass photometry reveals the dynamic oligomerization of human and plant peroxiredoxins.

ABSTRACT: Protein oligomerization is central to biological function and regulation, yet its experimental quantification and measurement of dynamic transitions in solution remain challenging. Here, we show that single molecule mass photometry quantifies affinity and polydispersity of heterogeneous protein complexes in solution. We demonstrate these capabilities by studying the functionally relevant oligomeric equilibria of 2-cysteine peroxiredoxins (2CPs). Comparison of the polydispersity of plant and human 2CPs as a function of concentration and redox state revealed features conserved among all 2CPs. In addition, we also find species-specific differences in oligomeric transitions, the occurrence of intermediates and the formation of high molecular weight complexes, which are associated with chaperon

SUBMITTER: Liebthal M 

PROVIDER: S-EPMC8571717 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature