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ABSTRACT: Background
Biomolecular condensates are non-stoichiometric assemblies that are characterized by their capacity to spatially concentrate biomolecules and play a key role in cellular organization. Proteins that drive the formation of biomolecular condensates frequently contain oligomerization domains and intrinsically disordered regions (IDRs), both of which can contribute multivalent interactions that drive higher-order assembly. Our understanding of the relative and temporal contribution of oligomerization domains and IDRs to the material properties of in vivo biomolecular condensates is limited. Similarly, the spatial and temporal dependence of protein oligomeric state inside condensates has been largely unexplored in vivo.Methods
In this study, we combined quantitative mi
SUBMITTER: Emenecker RJ
PROVIDER: S-EPMC8178893 | biostudies-literature | 2021 Jun
REPOSITORIES: biostudies-literature