{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Dey S"],"funding":["National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["6310-6323"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9561007"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["18(10)"],"pubmed_abstract":["For intrinsically disordered proteins (IDPs), a pressing question is how sequence codes for function. Dynamics serves as a crucial link, reminiscent of the role of structure in sequence-function relations of structured proteins. To define general rules governing sequence-dependent backbone dynamics, we carried out long molecular dynamics simulations of eight IDPs. Blocks of residues exhibiting large amplitudes in slow dynamics are rigidified by local inter-residue interactions or secondary structures. A long region or an entire IDP can be slowed down by long-range contacts or secondary-structure packing. On the other hand, glycines promote fast dynamics and either demarcate rigid blocks or facilitate multiple modes of local and long-range inter-residue interactions. The sequence-dependent backbone dynamics endows IDPs with versatile response to binding partners, with some blocks recalcitrant while others readily adapting to intermolecular interactions."],"journal":["Journal of chemical theory and computation"],"pubmed_title":["Sequence-Dependent Backbone Dynamics of Intrinsically Disordered Proteins."],"pmcid":["PMC9561007"],"funding_grant_id":["R35 GM118091"],"pubmed_authors":["Dey S","MacAinsh M","Zhou HX"],"additional_accession":[]},"is_claimable":false,"name":"Sequence-Dependent Backbone Dynamics of Intrinsically Disordered Proteins.","description":"For intrinsically disordered proteins (IDPs), a pressing question is how sequence codes for function. Dynamics serves as a crucial link, reminiscent of the role of structure in sequence-function relations of structured proteins. To define general rules governing sequence-dependent backbone dynamics, we carried out long molecular dynamics simulations of eight IDPs. Blocks of residues exhibiting large amplitudes in slow dynamics are rigidified by local inter-residue interactions or secondary structures. A long region or an entire IDP can be slowed down by long-range contacts or secondary-structure packing. On the other hand, glycines promote fast dynamics and either demarcate rigid blocks or facilitate multiple modes of local and long-range inter-residue interactions. The sequence-dependent backbone dynamics endows IDPs with versatile response to binding partners, with some blocks recalcitrant while others readily adapting to intermolecular interactions.","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Oct","modification":"2025-04-26T13:29:26.782Z","creation":"2025-04-06T14:16:02.533Z"},"accession":"S-EPMC9561007","cross_references":{"pubmed":["36084347"],"doi":["10.1021/acs.jctc.2c00328"]}}