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Role of Strong Localized vs Weak Distributed Interactions in Disordered Protein Phase Separation by Shiv Rekhi; Dinesh Sundaravadivelu Devarajan; Michael P. Howard; Young C. Kim; Arash Nikoubashman; Jeetain Mittal is a Chemistry article available to read on EtoBox.

What is Role of Strong Localized vs Weak Distributed Interactions in Disordered Protein Phase Separation about?

Interaction strength and localization are critical parameters controlling the single-chain and condensed-state properties of intrinsically disordered proteins (IDPs). Here, we decipher these relationships using coarse-grained heteropolymers comprised of hydrophobic (H) and polar (P) monomers as model IDPs. We systematically vary the fraction of P monomers __X__~P~ and employ two distinct particle-based models that include either strong localized attractions between only H–H pairs (HP model) or weak distributed attractions between both H–H and H–P pairs (HP+ model). To compare different sequences and models, we first carefully tune the attraction strength for all sequences to match the single-chain radius of gyration. Interestingly, we find that this procedure produces similar conformational ensembles, nonbonded potential energies, and chain-level dynamics for single chains of almost all sequences in both models, with some deviations for the HP model at large __X__~P~. However, we observe a surprisingly rich phase behavior for the sequences in both models that deviates from the expectation that similarity at the single-chain level will translate to a similar phase-separation propens

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Author

Shiv Rekhi; Dinesh Sundaravadivelu Devarajan; Michael P. Howard; Young C. Kim; Arash Nikoubashman; Jeetain Mittal

Publisher

American Chemical Society (ACS)

Published

2023

Language

EN

Field

Chemistry (Physical Sciences)