Titlebook: Neutrons in Biology; Benno P. Schoenborn Book 1984 Springer Science+Business Media New York 1984 life sciences

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Neutron Scattering Studies of the H2a-H2b and (H3-H4)2 Histone Complexes and some RNA. Its basic structural unit, the nucleosome (34), is formed by the interaction of the DNA with a class of basic proteins, the histones. This subunit is repeated along the chromatin fibers like beads on a string. It represents the first in a series of levels of folding of chromosomal DNA

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The Crystal Structure of the Nucleosome Core Particle by Contrast Variatione digestion of chromatin and consists of about equal weights of DNA (146 base pairs) and protein (an octamer of two pairs each of the histones H2A, H2B, H3, and H4). Nucleosome structure has been reviewed by McGhee and Felsenfeld (6). Studies by small-angle neutron scattering using D.O/H.O contrast

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A New Neutron Small-Angle Diffraction Instrument at the Brookhaven High Flux Beam Reactorhave made available an intense long wavelength neutron source that is ideally suited for the investigation of complex biological structures (1). This development and the more recent increase in reactor power to 60 MW encouraged the construction of a new small-angle neutron diffraction instrument.

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Neutron Diffraction Studies on Incorporation of Hexane into Oriented Lipid Bilayers as aggregates in a quasi-two-dimensional lipid bilayer matrix. Such molecules, which are strongly partitioned into the bilayer interior, must form mixtures of some type with the alkyl chains. It thus seems reasonable to view the membrane as a quasi-two-dimensional solution of lipids and proteins (2

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Specific Deuteration and Membrane Structures been obtained, mainly by x-ray diffraction, and some overall mean conformational properties of lipids have been determined (6, 10, 11, 13, 19, 20). As outlined by Tardieu et al. (20), one remarkable feature of lipids is their ability to combine in one phase a periodically ordered long-range organiz

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