Results 211 to 220 of about 186,634 (241)
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Shape analysis of the histone octamer in solution.
Science, 1986The conformation of the histone octamer is shown to depend upon the specific salt used to solubilize it. In 2 M sodium chloride the octamer is similar in size and shape to the histone component of crystallized core nucleosomes.
E. Uberbacher +3 more
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The histone octamer, a conformationally flexible structure.
Biochemistry, 1987The conformation of the histone octamer complex in solution has been shown, by circular dichroism studies, to be highly dependent on the nature of the salt milieu and its concentration. In 2 M NaCl, the complex has 43.5% alpha-helix, 16% beta-sheet, and 40.5% random structure.
K. Park, G. Fasman
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Energetics and affinity of the histone octamer for defined DNA sequences.
Biochemistry, 2001Previous studies have compared the relative free energies for histone octamer binding to various DNA sequences; however, no reports of the equilibrium binding affinity of the octamer for unique sequences have been presented. It has been shown that nucleosome core particles (NCPs) dissociate into free DNA and histone octamers (or free histones) on ...
J. Gottesfeld, K. Luger
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Spectropolarimetric analysis of the core histone octamer and its subunits.
Biochemistry, 1990The secondary structure of the calf thymus core histone octamer, (H2A-H2B-H3-H4)2, and its two physiological subunits, the H2A-H2B dimer and (H3-H4)2 tetramer, was analyzed by ORD spectropolarimetry as a function of temperature and solvent ionic strength within the ranges of these experimental parameters where assembly of the core histone octamer ...
J. E. Godfrey +2 more
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Biochemistry, 2005
Using a novel competition assay to determine the relative strength of different histone octamer-binding sites, we have compared three natural and two synthetic sites. We show that the relative affinities of these sites for the histone octamer depend upon both the temperature and octamer concentration.
Chenyi Wu, A. Travers
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Using a novel competition assay to determine the relative strength of different histone octamer-binding sites, we have compared three natural and two synthetic sites. We show that the relative affinities of these sites for the histone octamer depend upon both the temperature and octamer concentration.
Chenyi Wu, A. Travers
semanticscholar +3 more sources
Chicken Erythrocyte Histone Octamer Preparation
Cold Spring Harbor Protocols, 2008INTRODUCTIONCore histones can be purified from a variety of cell sources, including Drosophila embryos, HeLa tissue culture cells, calf thymus, or chicken erythrocytes. Chick erythrocytes are an excellent source of cellular histones: Large quantities of source material are readily obtainable, the purified histones have low levels of post-translational ...
Craig L, Peterson, Jeffrey C, Hansen
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Preparation of fluorescently labelled hybrid histone octamers
Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1990Labelling hybrid histone octamers (the Cys variant of histone H4 replaced histone H4 in the chicken erythrocyte octamer) with the fluorescent probe 5-(2(iodoacetyl)aminoethyl)aminonapthalene- 1-sulfonic acid, IAEDANS, resulted in significant non-specific incorporation of label.
G G, Lindsey, P, Thompson
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Characterization of the octamer of histones free in solution
Journal of Molecular Biology, 1977Abstract The nucleosome “core protein” isolated from chromatin in high-salt solutions (2 m -NaCl) has been characterized in detail. The preparation described yields material which is stable for prolonged periods at either 4 °C or 37 °C. It has an apparent partial specific volume of 0.767 ml/g and a sedimentation coefficient (S20,w0) of 4.77 (±0.04 ...
J O, Thomas, P J, Butler
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ESR studies of γ-irradiated histone octamer and the histone H3
Radiation Physics and Chemistry, 1998Abstract ESR spectrum of neat histone H3 γ -irradiated and observed at 77 K with low microwave power and modulation amplitude showed multiple resolved structure depicting nonequivalent interaction of the unpaired electron located at amido-carbonyl radical anion [– CHR C ( O − )NH–] of the peptide backbone with adjacent –NH– group and ...
Weizhen Lin +4 more
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Histone H2B (and H2A) ubiquitination allows normal histone octamer and core particle reconstitution
Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1994146 bp core particles were assembled from reconstituted hybrid histone octamers where either histone H2A or H2B were replaced by their ubiquitinated counterparts uH2A and uH2B. No difference in the structure of the core particles was evident upon DNase 1 digestion suggesting that ubiquitination of these histones was not a barrier to normal core ...
N, Davies, G G, Lindsey
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