en
Scientific article
English

Affinity and Valence Impact the Extent and Symmetry of Phase Separation of Multivalent Proteins

Published inPhysical review letters, vol. 129, no. 12, p. 1-6; 128102
Publication date2022-09-15
First online date2022-09-15
Abstract

Biomolecular self-assembly spatially segregates proteins with a limited number of binding sites (valence) into condensates that coexist with a dilute phase. We develop a many-body lattice model for a three-component system of proteins with fixed valence in a solvent. We compare the predictions of the model to experimental phase diagrams that we measure in vivo, which allows us to vary specifically a binding site’s affinity and valency. We find that the extent of phase separation varies exponentially with affinity and increases with valency. Valency alone determines the symmetry of the phase diagram.

eng
Keywords
  • Phase separation
  • Organelle
Affiliation Not a UNIGE publication
Funding
  • European Commission - Infinite Protein Self-Assembly in Health and Disease [819318]
Citation (ISO format)
NANDI, Saroj Kumar et al. Affinity and Valence Impact the Extent and Symmetry of Phase Separation of Multivalent Proteins. In: Physical review letters, 2022, vol. 129, n° 12, p. 1–6. doi: 10.1103/PhysRevLett.129.128102
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Article (Submitted version)
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Article (Published version)
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Identifiers
ISSN of the journal0031-9007
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