This subproject is one of many research subprojects utilizing the resources provided by a Shared Instrumentation Grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the grant, which is not necessarily the institution for the investigator. DESCRIPTION (provided by applicant): 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.
| 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 |
