Funding is requested for an 800 MHz NMR CryoProbe to support the research of a group of NIH, NSF and DOE funded scientists at UCLA, this probe will be used to help solve the structures and dynamics of proteins, nucleic acids, DNA-protein, RNA-protein, and protein-protein complexes proposed for investigation by the major users. The research projects of the six major users are described with the following titles: (1) NMR studies of proteins and their complexes (Clubb), (2) Structural studies of nucleic acids and complexes (Feigon), (3) SAM domain structure and function (Bowie), (4) Structure/function of HIV-1 Vpr and HHR23A associated cellular proteins (Chen), (5) Regulation of phage lambda site-specific DMA recombination by Xis and Fis (Johnson), and (6) Chaos Control and Sensitivity Enhancement in Biomolecular NMR (Lin). The probe will be located in the UCLA-DOE NMR Technology Center. It will significantly improve the sensitivity of the Center's single 800 MHz spectrometer enabling a greater number of projects to benefit from access to this high-field instrument. ? ?

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biomedical Research Support Shared Instrumentation Grants (S10)
Project #
1S10RR022471-01
Application #
7046272
Study Section
Special Emphasis Panel (ZRG1-BCMB-Q (30))
Program Officer
Tingle, Marjorie
Project Start
2006-04-01
Project End
2008-03-31
Budget Start
2006-04-01
Budget End
2008-03-31
Support Year
1
Fiscal Year
2006
Total Cost
$301,476
Indirect Cost
Name
University of California Los Angeles
Department
Genetics
Type
Schools of Medicine
DUNS #
092530369
City
Los Angeles
State
CA
Country
United States
Zip Code
90095
Sjodt, Megan; Macdonald, Ramsay; Marshall, Joanna D et al. (2018) Energetics underlying hemin extraction from human hemoglobin by Staphylococcus aureus. J Biol Chem 293:6942-6957
Sjodt, Megan; Macdonald, Ramsay; Spirig, Thomas et al. (2016) The PRE-Derived NMR Model of the 38.8-kDa Tri-Domain IsdH Protein from Staphylococcus aureus Suggests That It Adaptively Recognizes Human Hemoglobin. J Mol Biol 428:1107-1129
Chan, Albert H; Yi, Sung Wook; Terwilliger, Austen L et al. (2015) Structure of the Bacillus anthracis Sortase A Enzyme Bound to Its Sorting Signal: A FLEXIBLE AMINO-TERMINAL APPENDAGE MODULATES SUBSTRATE ACCESS. J Biol Chem 290:25461-74