Modulation of Intrinsically Disordered Protein Function by Post-translational Modifications.
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ABSTRACT: Post-translational modifications (PTMs) produce significant changes in the structural properties of intrinsically disordered proteins (IDPs) by affecting their energy landscapes. PTMs can induce a range of effects, from local stabilization or destabilization of transient secondary structure to global disorder-to-order transitions, potentially driving complete state changes between intrinsically disordered and folded states or dispersed monomeric and phase-separated states. Here, we discuss diverse biological processes that are dependent on PTM regulation of IDPs. We also present recent tools for generating homogenously modified IDPs for studies of PTM-mediated IDP regulatory mechanisms.
SUBMITTER: Bah A
PROVIDER: S-EPMC4807257 | biostudies-literature | 2016 Mar
REPOSITORIES: biostudies-literature
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