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- W2602413509 abstract "The roles of histone tails as substrates for reversible chemical modifications and dynamic cognate surfaces for the binding of regulatory proteins are well established. Despite these crucial roles, experimentally derived knowledge of the structure and possible binding sites of histone tails in chromatin is limited. In this study, we utilized molecular dynamics of isolated histone H3 N-terminal peptides to investigate its structure as a function of post-translational modifications that are known to be associated with defined chromatin states. We observed a structural preference for α-helices in isoforms associated with an inactive chromatin state, while isoforms associated with active chromatin states lacked α-helical content. The physicochemical effect of the post-translational modifications was highlighted by the interaction of arginine side-chains with the phosphorylated serine residues in the inactive isoform. We also showed that the isoforms exhibit different tail lengths, and, using molecular docking of the first 15 N-terminal residues of an H3 isoform, identified potential binding sites between the superhelical gyres on the octamer surface, close to the site of DNA entry/exit in the nucleosome. We discuss the possible functional role of the binding of the H3 tail within the nucleosome on both nucleosome and chromatin structure and stability." @default.
- W2602413509 created "2017-04-07" @default.
- W2602413509 creator A5045674634 @default.
- W2602413509 creator A5085152348 @default.
- W2602413509 date "2017-03-28" @default.
- W2602413509 modified "2023-10-14" @default.
- W2602413509 title "The effect of epigenetic modifications on the secondary structures and possible binding positions of the N-terminal tail of histone H3 in the nucleosome: a computational study" @default.
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- W2602413509 doi "https://doi.org/10.1007/s00894-017-3308-x" @default.
- W2602413509 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5391383" @default.
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