{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["8(9)"],"submitter":["Jacobs MI"],"pubmed_abstract":["Ordered supramolecular assemblies have recently been created using electrostatic interactions between oppositely charged proteins. Despite recent progress, the fundamental mechanisms governing the assembly of oppositely supercharged proteins are not fully understood. Here, we use a combination of experiments and computational modeling to systematically study the supramolecular assembly process for a series of oppositely supercharged green fluorescent protein variants. We show that net charge is a sufficient molecular descriptor to predict the interaction fate of oppositely charged proteins under a given set of solution conditions (e.g., ionic strength), but the assembled supramolecular structures critically depend on surface charge distributions. Interestingly, our results show that a larg"],"journal":["ACS central science"],"pagination":["1350-1361"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9523778"],"repository":["biostudies-literature"],"pubmed_title":["Understanding Supramolecular Assembly of Supercharged Proteins."],"pmcid":["PMC9523778"],"pubmed_authors":["Schroeder CM","Shukla D","Jacobs MI","Bansal P"],"additional_accession":[]},"is_claimable":false,"name":"Understanding Supramolecular Assembly of Supercharged Proteins.","description":"Ordered supramolecular assemblies have recently been created using electrostatic interactions between oppositely charged proteins. Despite recent progress, the fundamental mechanisms governing the assembly of oppositely supercharged proteins are not fully understood. Here, we use a combination of experiments and computational modeling to systematically study the supramolecular assembly process for a series of oppositely supercharged green fluorescent protein variants. We show that net charge is a sufficient molecular descriptor to predict the interaction fate of oppositely charged proteins under a given set of solution conditions (e.g., ionic strength), but the assembled supramolecular structures critically depend on surface charge distributions. Interestingly, our results show that a larg","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Sep","modification":"2025-04-22T03:40:14.322Z","creation":"2025-04-05T20:43:52.869Z"},"accession":"S-EPMC9523778","cross_references":{"pubmed":["36188338"],"doi":["10.1021/acscentsci.2c00730"]}}