Neutron scatter studies of chromatin structures related to functions. Technical progress report, November 1, 1991--May 15, 1992

Technical Report · Mon Jun 01 00:00:00 EDT 1992

DOI:https://doi.org/10.2172/10145857· OSTI ID:10145857

Bradbury, E M

We have made considerable progress in chromatin reconstitution with very lysine rich histone H1/H5 and in understanding the dynamics of nucleosomes. A ferromagnetic fluid was developed to align biological molecules for structural studies using small-angle-neutron-scattering. We have also identified and characterized in intrinsically bent DNA region flaking the RNA polymerase I binding site of the ribosomal RNA gene in Physarum Polycephalum. Finally projects in progress are in the areas of studying the interactions of histone H4 amino-terminus peptide 1-23 and acetylated 1-23 peptide with DNA using thermal denaturation; study of GGAAT repeats found in human centromeres using high resolution Nuclear Magnetic Resonance and nuclease sentivity assay; and the role of histones and other sperm specific proteins with sperm chromatin.

• Research Organization: California Univ., Davis, CA (United States)
• Sponsoring Organization: USDOE, Washington, DC (United States)
• DOE Contract Number: FG03-88ER60673
• OSTI ID: 10145857
• Report Number(s): DOE/ER/60673-T4; ON: DE92014032
• Resource Relation: Other Information: PBD: [1992]
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CHROMATIN
NEUTRON DIFFRACTION
PROGRESS REPORT
SMALL ANGLE SCATTERING
HISTONES
NUCLEOSOMES
ORIENTATION
FERROMAGNETIC MATERIALS
RNA POLYMERASES
550200
665100
BIOCHEMISTRY
NUCLEAR TECHNIQUES IN CONDENSED MATTER PHYSICS