NIH-funded principal investigators at the University of Maryland, Baltimore have a scientific need for a state-of-the-art 600 MHz NMR spectrometer console to carry out their NIH funded NMR-related research. This equipment is necessary to (i) become state-of-the art, (ii) to adequately protect our cryogenic probe and (iii) to reduce the amount of NMR down-time resulting from the high failure rate of our existing 600 MHz instrumentation. The users of the UMB NMR center include faculty members from the School of Medicine, the School of Pharmacy, the Greenebaum Cancer Center, the University of Maryland Biotechnology center, and users from other universities and private companies. The ongoing NIH-funded projects that are dependent upon the 600 MHz NMR spectrometer include: 1. Dr. David J. Weber (PI), Structure/function and drug design for S100 proteins; 2. Dr. Lindsay Black, Structure/function studies of the phage IPI protein; 3. Dr. Alex Drohat, The structure of the human TDG catalytic core by NMR spectroscopy; 4. Dr. A-Lien Lu-Chang, Structural and Mechanistic Studies of DNA Mismatch Repair Proteins, 5. Dr. Frank Margolis, Structure/function studies of OMP bound to the Bex proteins; 6. Dr. Mary McKenna, Monocarboxylic acids and amino acids in metabolism and trafficking in the brain; 7. Dr. James Nataro, Structure/Function studies of Dispersin; 8. Dr. Kristen Varney, Structure and Function of Mts1 (S100A4). In addition, four other projects are briefly described in this application, which also have an essential need for continued use of the 600 MHz NMR spectrometer. ? ? Relevance: The ongoing NMR-related projects under study by NIH-funded principal investigators at the University of Maryland, Baltimore address many important public health concerns including cancer, HIV/AIDS, aging, heart disease, and several aspects of drug design. ? ? ?

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biomedical Research Support Shared Instrumentation Grants (S10)
Project #
1S10RR023447-01
Application #
7212707
Study Section
Special Emphasis Panel (ZRG1-BCMB-K (30))
Program Officer
Tingle, Marjorie
Project Start
2007-04-01
Project End
2008-03-31
Budget Start
2007-04-01
Budget End
2008-03-31
Support Year
1
Fiscal Year
2007
Total Cost
$362,400
Indirect Cost
Name
University of Maryland Baltimore
Department
Biochemistry
Type
Schools of Medicine
DUNS #
188435911
City
Baltimore
State
MD
Country
United States
Zip Code
21201
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Roth, Braden M; Varney, Kristen M; Rustandi, Richard R et al. (2016) (1)H(N), (13)C, and (15)N resonance assignments of the CDTb-interacting domain (CDTaBID) from the Clostridium difficile binary toxin catalytic component (CDTa, residues 1-221). Biomol NMR Assign 10:335-9
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