{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Nguyen A"],"funding":["Intramural NIH HHS","NIH HHS"],"pagination":["RP94836"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11213569"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13"],"pubmed_abstract":["Genetic diversity is a hallmark of RNA viruses and the basis for their evolutionary success. Taking advantage of the uniquely large genomic database of SARS-CoV-2, we examine the impact of mutations across the spectrum of viable amino acid sequences on the biophysical phenotypes of the highly expressed and multifunctional nucleocapsid protein. We find variation in the physicochemical parameters of its extended intrinsically disordered regions (IDRs) sufficient to allow local plasticity, but also observe functional constraints that similarly occur in related coronaviruses. In biophysical experiments with several N-protein species carrying mutations associated with major variants, we find that point mutations in the IDRs can have nonlocal impact and modulate thermodynamic stability, secondar"],"journal":["eLife"],"pubmed_title":["Modulation of biophysical properties of nucleocapsid protein in the mutant spectrum of SARS-CoV-2."],"pmcid":["PMC11213569"],"funding_grant_id":["ZIA EB000099","ZIA EB000099-02"],"pubmed_authors":["Schuck P","Chen J","Srinivasan S","Nguyen A","Myagmarsuren D","Wu D","Piszczek G","Zhao H"],"additional_accession":[]},"is_claimable":false,"name":"Modulation of biophysical properties of nucleocapsid protein in the mutant spectrum of SARS-CoV-2.","description":"Genetic diversity is a hallmark of RNA viruses and the basis for their evolutionary success. Taking advantage of the uniquely large genomic database of SARS-CoV-2, we examine the impact of mutations across the spectrum of viable amino acid sequences on the biophysical phenotypes of the highly expressed and multifunctional nucleocapsid protein. We find variation in the physicochemical parameters of its extended intrinsically disordered regions (IDRs) sufficient to allow local plasticity, but also observe functional constraints that similarly occur in related coronaviruses. In biophysical experiments with several N-protein species carrying mutations associated with major variants, we find that point mutations in the IDRs can have nonlocal impact and modulate thermodynamic stability, secondar","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jun","modification":"2026-05-29T16:52:36.429Z","creation":"2026-04-08T05:27:37.284Z"},"accession":"S-EPMC11213569","cross_references":{"pubmed":["38941236"],"doi":["10.7554/eLife.94836"]}}