Proximity to criticality predicts surface properties of biomolecular condensates.

biomolecular condensates critical phenomena molecular-dynamics phase separation surface tension

Journal

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876

Informations de publication

Date de publication:
06 06 2023
Historique:
medline: 1 6 2023
pubmed: 30 5 2023
entrez: 30 5 2023
Statut: ppublish

Résumé

It has recently become appreciated that cells self-organize their interiors through the formation of biomolecular condensates. These condensates, typically formed through liquid-liquid phase separation of proteins, nucleic acids, and other biopolymers, exhibit reversible assembly/disassembly in response to changing conditions. Condensates play many functional roles, aiding in biochemical reactions, signal transduction, and sequestration of certain components. Ultimately, these functions depend on the physical properties of condensates, which are encoded in the microscopic features of the constituent biomolecules. In general, the mapping from microscopic features to macroscopic properties is complex, but it is known that near a critical point, macroscopic properties follow power laws with only a small number of parameters, making it easier to identify underlying principles. How far does this critical region extend for biomolecular condensates and what principles govern condensate properties in the critical regime? Using coarse-grained molecular-dynamics simulations of a representative class of biomolecular condensates, we found that the critical regime can be wide enough to cover the full physiological range of temperatures. Within this critical regime, we identified that polymer sequence influences surface tension predominately via shifting the critical temperature. Finally, we show that condensate surface tension over a wide range of temperatures can be calculated from the critical temperature and a single measurement of the interface width.

Identifiants

pubmed: 37252985
doi: 10.1073/pnas.2220014120
pmc: PMC10266063
doi:

Substances chimiques

Proteins 0
Nucleic Acids 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

e2220014120

Subventions

Organisme : HHS | NIH | National Institute of General Medical Sciences (NIGMS)
ID : R01GM140032

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Auteurs

Andrew G T Pyo (AGT)

Department of Physics, Princeton University, Princeton, NJ 08544.

Yaojun Zhang (Y)

Department of Physics, Princeton University, Princeton, NJ 08544.
Department of Physics and Astronomy, Johns Hopkins University, Baltimore, MD 21218.
Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218.
Lewis-Sigler Institute for Integrative Genomics, Princeton University, Princeton, NJ 08544.

Ned S Wingreen (NS)

Lewis-Sigler Institute for Integrative Genomics, Princeton University, Princeton, NJ 08544.
Department of Molecular Biology, Princeton University, Princeton, NJ 08544.

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Classifications MeSH