{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hicks A"],"funding":["National Institutes of Health"],"pagination":["E946"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7355643"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10(6)"],"pubmed_abstract":["How sequences of intrinsically disordered proteins (IDPs) code for their conformational dynamics is poorly understood. Here, we combined NMR spectroscopy, small-angle X-ray scattering (SAXS), and molecular dynamics (MD) simulations to characterize the conformations and dynamics of ChiZ1-64. MD simulations, first validated by SAXS and secondary chemical shift data, found scant α-helices or β-strands but a considerable propensity for polyproline II (PPII) torsion angles. Importantly, several blocks of residues (e.g., 11-29) emerge as \"correlated segments\", identified by their frequent formation of PPII stretches, salt bridges, cation-π interactions, and sidechain-backbone hydrogen bonds. NMR relaxation experiments showed non-uniform transverse relaxation rates (R2s) and nuclear Overhauser enhancements (NOEs) along the sequence (e.g., high R2s and NOEs for residues 11-14 and 23-28). MD simulations further revealed that the extent of segmental correlation is sequence-dependent; segments where internal interactions are more prevalent manifest elevated \"collective\" motions on the 5-10 ns timescale and suppressed local motions on the sub-ns timescale. Amide proton exchange rates provides corroboration, with residues in the most correlated segment exhibiting the highest protection factors. We propose the correlated segment as a defining feature for the conformations and dynamics of IDPs."],"journal":["Biomolecules"],"pubmed_title":["Sequence-Dependent Correlated Segments in the Intrinsically Disordered Region of ChiZ."],"pmcid":["PMC7355643"],"funding_grant_id":["GM118091; AI119178"],"pubmed_authors":["Escobar CA","Cross TA","Zhou HX","Hicks A"],"additional_accession":[]},"is_claimable":false,"name":"Sequence-Dependent Correlated Segments in the Intrinsically Disordered Region of ChiZ.","description":"How sequences of intrinsically disordered proteins (IDPs) code for their conformational dynamics is poorly understood. Here, we combined NMR spectroscopy, small-angle X-ray scattering (SAXS), and molecular dynamics (MD) simulations to characterize the conformations and dynamics of ChiZ1-64. MD simulations, first validated by SAXS and secondary chemical shift data, found scant α-helices or β-strands but a considerable propensity for polyproline II (PPII) torsion angles. Importantly, several blocks of residues (e.g., 11-29) emerge as \"correlated segments\", identified by their frequent formation of PPII stretches, salt bridges, cation-π interactions, and sidechain-backbone hydrogen bonds. NMR relaxation experiments showed non-uniform transverse relaxation rates (R2s) and nuclear Overhauser enhancements (NOEs) along the sequence (e.g., high R2s and NOEs for residues 11-14 and 23-28). MD simulations further revealed that the extent of segmental correlation is sequence-dependent; segments where internal interactions are more prevalent manifest elevated \"collective\" motions on the 5-10 ns timescale and suppressed local motions on the sub-ns timescale. Amide proton exchange rates provides corroboration, with residues in the most correlated segment exhibiting the highest protection factors. We propose the correlated segment as a defining feature for the conformations and dynamics of IDPs.","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Jun","modification":"2025-04-26T08:14:54.229Z","creation":"2025-04-06T12:37:20.991Z"},"accession":"S-EPMC7355643","cross_references":{"pubmed":["32585849"],"doi":["10.3390/biom10060946"]}}