{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Rabdano SO"],"funding":["Saint Petersburg State University","National Institutes of Health","Russian Science Foundation","NIGMS NIH HHS","NIH HHS","National Science Foundation"],"pagination":["6480-6487"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7994933"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["60(12)"],"pubmed_abstract":["The interaction of positively charged N-terminal histone tails with nucleosomal DNA plays an important role in chromatin assembly and regulation, modulating their susceptibility to post-translational modifications and recognition by chromatin-binding proteins. Here, we report residue-specific <sup>15</sup> N NMR relaxation rates for histone H4 tails in reconstituted nucleosomes. These data indicate that H4 tails are strongly dynamically disordered, albeit with reduced conformational flexibility compared to a free peptide with the same sequence. Remarkably, the NMR observables were successfully reproduced in a 2-μs MD trajectory of the nucleosome. This is an important step toward resolving an apparent inconsistency where prior simulations were generally at odds with experimental evidence on"],"journal":["Angewandte Chemie (International ed. in English)"],"pubmed_title":["Histone H4 Tails in Nucleosomes: a Fuzzy Interaction with DNA."],"pmcid":["PMC7994933"],"funding_grant_id":["MCB-1715174","S10 OD012303","R01GM123743","15-14-20038","R01GM118664","R01 GM123743","S10OD012303","51142660","R01 GM118664"],"pubmed_authors":["Gonzalez Salguero N","Jaroniec CP","Purusottam RN","Skrynnikov NR","Rabdano SO","Izmailov SA","Shannon MD","Poirier MG","Zandian M"],"additional_accession":[]},"is_claimable":false,"name":"Histone H4 Tails in Nucleosomes: a Fuzzy Interaction with DNA.","description":"The interaction of positively charged N-terminal histone tails with nucleosomal DNA plays an important role in chromatin assembly and regulation, modulating their susceptibility to post-translational modifications and recognition by chromatin-binding proteins. Here, we report residue-specific <sup>15</sup> N NMR relaxation rates for histone H4 tails in reconstituted nucleosomes. These data indicate that H4 tails are strongly dynamically disordered, albeit with reduced conformational flexibility compared to a free peptide with the same sequence. Remarkably, the NMR observables were successfully reproduced in a 2-μs MD trajectory of the nucleosome. This is an important step toward resolving an apparent inconsistency where prior simulations were generally at odds with experimental evidence on","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Mar","modification":"2026-05-31T07:06:26.917Z","creation":"2025-04-05T09:50:13.695Z"},"accession":"S-EPMC7994933","cross_references":{"pubmed":["33522067"],"doi":["10.1002/anie.202012046"]}}