NMR studies on the N-terminal acetylation domain of histone H4

E. Bang, C. H. Lee, J. B. Yoon, J. Chung, Woon Lee Dai Woon Lee, W. Lee

Research output: Contribution to journalArticle

1 Citation (Scopus)

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 H4NTP 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 H4NTP prefers an extended backbone conformation at acetylation sites, however, it (especially Lys12) became more defined structures after acetylation for its optimum function.

Original languageEnglish
Pages (from-to)507-513
Number of pages7
JournalBulletin of the Korean Chemical Society
Volume22
Issue number5
Publication statusPublished - 2001 May 20

All Science Journal Classification (ASJC) codes

  • Chemistry(all)

Fingerprint Dive into the research topics of 'NMR studies on the N-terminal acetylation domain of histone H4'. Together they form a unique fingerprint.

  • Cite this