{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["34(2)"],"submitter":["Italia V"],"funding":["Cotutelle Fellowship from the ubBIO project","IDEX Strategic Alliance between University Grenoble Alpes (France) and Swansea University (UK)","National Institutes of Health","NIH HHS"],"pubmed_abstract":["The Drosophila intrinsically disordered protein Ultrabithorax (Ubx) undergoes a series of phase transitions, beginning with noncovalent interactions between apparently randomly organized monomers, and evolving over time to form increasingly ordered coacervates. This assembly process ends when specific dityrosine covalent bonds lock the monomers in place, forming macroscale materials. Inspired by this hierarchical, multistep assembly process, we analyzed the impact of protein concentration, assembly time, and subphase composition on the early, noncovalent stages of Ubx assembly, which are extremely sensitive to their environment. We discovered that in low salt buffers, we can generate a new type of Ubx material from early coacervates using 5-fold less protein, and 100-fold less assembly tim"],"journal":["Protein science : a publication of the Protein Society"],"pagination":["e70000"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11751906"],"repository":["biostudies-literature"],"pubmed_title":["Chemical and temporal manipulation of early steps in protein assembly tunes the structure and intermolecular interactions of protein-based materials."],"pmcid":["PMC11751906"],"pubmed_authors":["Bondos SE","Kaparthi B","Italia V","Maccarini M","Faulk B","Martin DK","Bertoncello P","Meissner K","Jons A"],"additional_accession":[]},"is_claimable":false,"name":"Chemical and temporal manipulation of early steps in protein assembly tunes the structure and intermolecular interactions of protein-based materials.","description":"The Drosophila intrinsically disordered protein Ultrabithorax (Ubx) undergoes a series of phase transitions, beginning with noncovalent interactions between apparently randomly organized monomers, and evolving over time to form increasingly ordered coacervates. This assembly process ends when specific dityrosine covalent bonds lock the monomers in place, forming macroscale materials. Inspired by this hierarchical, multistep assembly process, we analyzed the impact of protein concentration, assembly time, and subphase composition on the early, noncovalent stages of Ubx assembly, which are extremely sensitive to their environment. We discovered that in low salt buffers, we can generate a new type of Ubx material from early coacervates using 5-fold less protein, and 100-fold less assembly tim","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Feb","modification":"2026-06-06T19:41:15.964Z","creation":"2026-06-04T03:11:42.726Z"},"accession":"S-EPMC11751906","cross_references":{"pubmed":["39840718"],"doi":["10.1002/pro.70000"]}}