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Homo- and heteronuclear two-dimensional NMR studies of the globular domain of histone H1: sequential assignment and secondary structure
Publication Type:
Journal ArticleSource:
Volume 32, Issue 42, p.11345 - 11351 (1993)URL:
PM:8218199Keywords:
Amino Acid Sequence; Animals; Chickens; Erythrocytes; metabolism; Genes; Synthetic; Histones; chemistry; isolation & purification; Magnetic Resonance Spectroscopy; methods; Models; Structural; Molecular Sequence Data; Protein Structure; Secondary; RecombinanAbstract:
A recombinant 75 amino acid polypeptide corresponding to the globular domain of the chicken histone H1 (GH1) has been studied by 1H homonuclear and 1H-15N heteronuclear 2D NMR spectroscopy. Sequential assignment of the backbone and beta-proton resonances has enabled us to determine the secondary structure of GH1. It was found to consist of three helical regions (T7-S17, L25-Y37, E40-K56) and probably a beta-hairpin (L59-L73). This structure is similar to the structure of the globular domain of histone H5 (GH5) obtained both by NMR spectroscopy [Zarbock et al. (1986) Proc. Natl. Acad. Sci. U.S.A. 83, 7628-7632; Clore et al. (1987) EMBO J. 6, 1833-1842] and by X-ray crystallography [Ramakrishnan et al. (1993) Nature 362, 219-223]. The beta-hairpin as suggested for GH1 is also present in the X-ray structure of GH5 but has not been reported for the NMR structure of GH5
Notes:
DA - 19931126
IS - 0006-2960 (Print)
LA - eng
PT - Comparative Study
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
PT - Research Support, U.S. Gov't, Non-P.H.S
PT - Research Support, U.S. Gov't, P.H.S
RN - 0 (Histones)
RN - 0 (Recombinant Proteins)
SB - IM