|Title||Homo- and heteronuclear two-dimensional NMR studies of the globular domain of histone H1: sequential assignment and secondary structure.|
|Publication Type||Journal Article|
|Year of Publication||1993|
|Authors||Cerf, C., G. Lippens, S. Muyldermans, A. Segers, V. Ramakrishnan, S. J. Wodak, K. Hallenga, and L. Wyns|
|Date Published||1993 Oct 26|
|Keywords||Amino Acid Sequence, Animals, Chickens, Erythrocytes, Genes, Synthetic, Histones, Magnetic Resonance Spectroscopy, Models, Structural, Molecular Sequence Data, Protein Structure, Secondary, Recombinant Proteins|
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.
|Grant List||GM42796 / GM / NIGMS NIH HHS / United States|