Results 21 to 30 of about 50 (49)

Chromatin Stability at Low Concentration Depends on Histone Octamer Saturation Levels [PDF]

Biophysical Journal, 2009
Studies on the stability of nucleosome core particles as a function of concentration have indicated a lower limit of approximately 5 ng/microL, below which the complexes start to spontaneously destabilize. Until recently little information was available on the effect of low concentration on chromatin.
James Denvir, Qiang Fu, Benoit Molinié, Thomas A. HagermanT.A. Hagerman, Philippe T. Georgel, Stuart Lindsay   +5 more
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The exocyclic groups of DNA modulate the affinity and positioning of the histone octamer [PDF]

Proceedings of the National Academy of Sciences, 1998
To investigate the nature of the chemical determinants in DNA required for nonspecific binding and bending by proteins we have created a novel DNA in which inosine–5-methylcytosine and 2,6-diaminopurine–uracil base pairs are substituted for normal base pairs in a defined DNA sequence.
Memmo Buttinelli, Michael J. Waring, Gianna Panetta, Andrew Travers, Andrew Minnock   +4 more
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Neutron and x-ray scatter studies of the histone octamer and amino and carboxyl domain trimmed octamers.

Journal of Biological Chemistry, 1991
The structure of the nucleosome has been under intense investigation using neutron crystallography, x-ray crystallography, and neutron solution scattering. However the dimension of the histone octamer inside the nucleosome is still a subject of controversy.
A G Fowler, Martin W. Goldberg, Peter M. Yau, S J Lambert, B S Imai, J E Godfrey, M J Wood, E N Moudrianakis, M H Koch, J. P. Baldwin   +9 more
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High Energy Radiation-Induced Crosslinking of Histone Octamer Complexes

Zeitschrift für Naturforschung C, 1984
Abstract Calf thymus histone octamer complexes were irradiated in the native state in N2O-saturated dilute aqueous solution (0.5 g/l, pH 9, [NaClO4] = 1-4 mol/1) with 50 or 100 ns pulses of 16 MeV electrons or 60Co-γ-rays. Tim e resolved light scattering measurem ents and optical ab­sorption measurements yielded the following: the ...
L. Katsikas, K.-J. Deeg, W. Schnabel
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Crystallographic Structure of the Octamer Histone Core of the Nucleosome [PDF]

Science, 1985
Edward C. Uberbacher, Gerard J. Bunick
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Chicken Erythrocyte Histone Octamer Preparation

Cold Spring Harbor Protocols, 2008
INTRODUCTIONCore 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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The histone octamer, a conformationally flexible structure

Biochemistry, 1987
The 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.
Kyusung Park, Gerald D. Fasman
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Characterization of the octamer of histones free in solution

Journal of Molecular Biology, 1977
Abstract 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 ...
Jean O. Thomas, Jean O. Thomas, P.J.G. Butler, P.J.G. Butler   +3 more
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Shape Analysis of the Histone Octamer in Solution

Science, 1986
The 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.
Gerard J. Bunick, E. Wilkinson-Singley, Edward C. Uberbacher, Joel M. Harp   +3 more
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Preparation of fluorescently labelled hybrid histone octamers

Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1990
Labelling 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.
Patricia Thompson, George G. Lindsey
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