reviewJournal of Biological ChemistryFeb 6, 2016HYBRID OA

Modulation of Intrinsically Disordered Protein Function by Post-translational Modifications

University of Toronto · Hospital for Sick Children

PubMed
Indexed incrossrefdoajpubmed

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.

Citation impact

575
total citations
FWCI
24.02
Percentile
100%
References
101
Citations per year

Authors

2

Topics & keywords

Keywords
  • Intrinsically disordered proteins
  • Function (biology)
  • Modulation (music)
  • Biophysics
  • Posttranslational modification
  • Chemistry
  • Cell biology
  • Physics
UN Sustainable Development Goals
  • Affordable and clean energy
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