NIH-funded principal investigators at the University of Maryland, Baltimore (UMB), the University of Maryland, Baltimore County (UMBC), and the University of Maryland, College Park (UMCP) have scientific need for a state-of-the-art shielded 950 MHz NMR because of an increasing number of biomolecular NMR-based research projects. This instrument will be located in specially designed space in the UMB NMR shared core facility, which is fully ready to house this instrumentation ( The University of Maryland has committed to providing the resources necessary to properly install and operate this new shared resource and salary support for the facility manager, Dr. Kristen Varney. The administration of the 950 MHz NMR and its shared operation are set by a committee that includes Drs. David J. Weber (UMB), Michael Summers (UMBC), David Fushman (UMCP) and Kristen Varney (UMB). The NIH-funded principle investigators (PIs) that have a need for a 950 MHz NMR spectrometer include: 1. Dr. David J. Weber (UMB), Structure/function and inhibition of protein-protein complexes involving S100 proteins;2. Dr. Michael Summers (UMBC) NMR studies of retroviral genome packaging;3. Dr. David Fushman (UMCP) Solution structure and dynamics of polyubiquitin chains;4. Dr. Kwaku Dayie (UMCP) Molecular recognition: structural and dynamic basis for RNA-macromolecular interactions in gene regulation and catalysis;5. Dr. Bruce Johnson (UMBC) Continued development and maintenance of NMRview;6. Dr. Alex Drohat (UMB), Structure of CpG specific DNA glycosylases;7. Dr. Frank Margolis (UMB), Structure/function studies of OMP and its influence on the Na?exchanger (NCX);8. Dr. James Nataro (UMB), Structure/function studies of dispersin and of the AAF family of fimbraie;and 9. Dr. Kristen Varney (UMB, Manager), Protein-protein complexes involving the metastasis protein 1. Dr. Vitali Tugarinov (project 10;Title: """"""""Development of NMR and isotope labeling methodology for the studies of structure and dynamics of high molecular weight proteins) was recently hired at the University of Maryland (UMCP), so he as well as twelve additional investigators (projects 11-21) with new/representative projects are included in the application. Projects for fourteen other investigators (projects 22-35) who have used the NMR center in the past and could have future need for a state-of-the-art 950 MHz NMR spectrometer are also listed. As in the past, we will make the 950 MHz NMR available to other PIs in the Mid-Atlantic region as well as throughout the United States, upon request. Because of an NIGMS funded IMSD PhD program (PI: Michael Summers), underrepresented minority (URM) participation in the UMBC/UMB Biochemistry program has jumped from 0 to 30% over the past 15 years. Thus, in addition to supporting the NIH funded research projects listed in this proposal and throughout the country, the requested resources will also provide top URM students at the University of Maryland with state-of the art training facilities.

Public Health Relevance

The ongoing NMR-related projects under study by NIH funded principal investigators at the University of Maryland, Baltimore (UMB), University of Maryland, Baltimore County (UMBC), and University of Maryland, College Park (UMCP) address many important public health concerns including cancer, HIV/AIDS, aging, heart disease, neuroscience, and several aspects of drug design

National Institute of Health (NIH)
National Center for Research Resources (NCRR)
Biomedical Research Support Shared Instrumentation Grants (S10)
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Study Section
Special Emphasis Panel (ZRG1-BCMB-N (30))
Program Officer
Levy, Abraham
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University of Maryland Baltimore
Schools of Medicine
United States
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Roth, Braden M; Godoy-Ruiz, Raquel; Varney, Kristen M et al. (2016) 1H, 13C, and 15N resonance assignments of an enzymatically active domain from the catalytic component (CDTa, residues 216-420) of a binary toxin from Clostridium difficile. Biomol NMR Assign 10:213-7
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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