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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 22, Number 5
BKCSDE 22(5)
May 20, 2001

Title	NMR Studies on the N-Terminal Acetylation Domain of Histone H4
Author	Eunjung Bang, Chang-Hun Lee, Jong-Bok Yoon, Joohee Chung, Dai Woon Lee, Weontae Lee
Keywords	Histone H4, Acetylation, NMR structure.
Abstract	Histones, nuclear proteins that interact with DNA to form nucleosomes, are essential for both the regulation of transcription and the packaging of DNA within chromosomes. The N-terminal domain of histone H4 which contains four acetylation sites at lysines, may play a separate role in chromatin structure from the remainder of the H4 chain. NMR data suggest that H4^NTP peptide does have relating disordered structure at physiological pH, however, it has a defined structure at lower pH conditions. The solution structure calculated from NMR data shows a well structured region comprising residues of Val21-Asp24. In addition, our results suggest that the H4^NTP prefers an extended backbone conformation at acetylation sites, however, it (especially Lys ¹² ) became more defined structures after acetylation for its optimum function.
Page	507 - 513
Full Text	PDF

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