Proton NMR study on a type II DNA binding protein huα from escherichia coli and its complex with oligo DNA

H. Shindo, H. Kurumizaka, A. Furubayashi, C. Sakuma, U. Matumoto, A. Yanagida, N. Goshima, Y. Kano, F. Imamoto

研究成果: Article査読

抄録

The solution structures of HUα and its complex with oligo DNA were studied by proton NMR spectroscopy. It was confirmed that the arm region of HU forms antiparallel β-sheet and that all of the residues of phenylalanines together with some of leucines and/or valines form a hydrophobic core within the dimer of HU protein. Upon complex formation of HUα with DNA, several resonances from both HU and DNA were perturbed and the intermolecuar NOEs between HU and DNA were observed, suggesting that HU binds primarily to the minor groove of DNA.

本文言語English
ページ(範囲)849-852
ページ数4
ジャーナルAnalytical Sciences
7
Supplement
DOI
出版ステータスPublished - 1991
外部発表はい

ASJC Scopus subject areas

  • 分析化学

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