Phosphorylation of disordered proteins tunes local and global intramolecular interactions.

ABSTRACT: Protein post-translational modifications, such as phosphorylation, are important regulatory signals for diverse cellular functions. In particular, intrinsically disordered protein regions (IDRs) are subject to phosphorylation as a means to modulate their interactions and functions. Toward understanding the relationship between phosphorylation in IDRs and specific functional outcomes, we must consider how phosphorylation affects the IDR conformational ensemble. Various experimental techniques are suited to interrogate the features of IDR ensembles; molecular simulations can provide complementary insights and even illuminate ensemble features that may be experimentally inaccessible. Therefore, we sought to expand the tools available to study phosphorylated IDRs by all-atom Monte Carlo simula

SUBMITTER: Usher ET 

PROVIDER: S-EPMC11628823 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature