Neutron scatter studies of chromatin structures related to functions

Technical Report · Wed Jan 01 00:00:00 EST 1992

DOI:https://doi.org/10.2172/7224363· OSTI ID:7224363

Bradbury, E M

Despite of setbacks in the lack of neutrons for the proposed We have made considerable progress in chromatin reconstitution with the VLR 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 an intrinsically bent DNA region flanking 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 interatctions 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; USDOE, Washington, DC (United States)
• DOE Contract Number: FG03-88ER60673
• OSTI ID: 7224363
• Report Number(s): DOE/ER/60673-T5; ON: DE93002520
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
37 INORGANIC
ORGANIC
PHYSICAL AND ANALYTICAL CHEMISTRY
CHROMATIN
MOLECULAR STRUCTURE
NUCLEOSOMES
NEUTRON DIFFRACTION
TRANSCRIPTION FACTORS
HISTONES
PROGRESS REPORT
COHERENT SCATTERING
DIFFRACTION
DOCUMENT TYPES
SCATTERING
550200* - Biochemistry
550400 - Genetics
400101 - Activation
Nuclear Reaction
Radiometric & Radiochemical Procedures