Biomolecular condensate microstructure is invariant to sequence-encoded molecular and macroscopic properties.

ABSTRACT: Biomolecular condensates, including those formed by prion-like low complexity domains (LCDs) of proteins, are maintained by networks of molecular interactions. Such collective interactions give rise to the rich array of material behaviors underlying condensate function. Previous work has uncovered distinct LCD conformations in condensates versus dilute phases, and recently, single-component LCD condensates have been predicted to exhibit microstructures with "small-world" networks-where molecular nodes are highly clustered and connected via short pathlengths. However, a framework linking single-molecule properties, condensate microstructure, and macroscopic material properties remains elusive. Here, we combine molecular simulation and graph-theoretic analysis to reveal that sm

SUBMITTER: Tan D 

PROVIDER: S-EPMC12455476 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature