{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Sanchez-Burgos I"],"funding":["Derek Brewer Emmanuel College scholarship","European Research Council","Roger Ekins Fellowship","Oppenheimer Fellowship","Engineering and Physical Sciences Research Council"],"pagination":["e1009810"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8896709"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["18(2)"],"pubmed_abstract":["Biomolecular condensates formed via liquid-liquid phase separation (LLPS) play a crucial role in the spatiotemporal organization of the cell material. Nucleic acids can act as critical modulators in the stability of these protein condensates. To unveil the role of RNA length in regulating the stability of RNA binding protein (RBP) condensates, we present a multiscale computational strategy that exploits the advantages of a sequence-dependent coarse-grained representation of proteins and a minimal coarse-grained model wherein proteins are described as patchy colloids. We find that for a constant nucleotide/protein ratio, the protein fused in sarcoma (FUS), which can phase separate on its own-i.e., via homotypic interactions-only exhibits a mild dependency on the RNA strand length. In contra"],"journal":["PLoS computational biology"],"pubmed_title":["RNA length has a non-trivial effect in the stability of biomolecular condensates formed by RNA-binding proteins."],"pmcid":["PMC8896709"],"funding_grant_id":["EP/T517847/1","803326","EP/P020259/1"],"pubmed_authors":["Joseph JA","Espinosa JR","Sanchez-Burgos I","Collepardo-Guevara R"],"additional_accession":[]},"is_claimable":false,"name":"RNA length has a non-trivial effect in the stability of biomolecular condensates formed by RNA-binding proteins.","description":"Biomolecular condensates formed via liquid-liquid phase separation (LLPS) play a crucial role in the spatiotemporal organization of the cell material. Nucleic acids can act as critical modulators in the stability of these protein condensates. To unveil the role of RNA length in regulating the stability of RNA binding protein (RBP) condensates, we present a multiscale computational strategy that exploits the advantages of a sequence-dependent coarse-grained representation of proteins and a minimal coarse-grained model wherein proteins are described as patchy colloids. We find that for a constant nucleotide/protein ratio, the protein fused in sarcoma (FUS), which can phase separate on its own-i.e., via homotypic interactions-only exhibits a mild dependency on the RNA strand length. In contra","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Feb","modification":"2025-04-05T11:08:21.646Z","creation":"2025-04-05T11:08:21.646Z"},"accession":"S-EPMC8896709","cross_references":{"pubmed":["35108264"],"doi":["10.1371/journal.pcbi.1009810"]}}