Support is requested to acquire a high-sensitivity 600 MHz triple resonance (1H, 13C, 15N) TCI cryoprobe and to upgrade an existing 600 MHz (1H Larmor frequency) NMR spectrometer console at Montana State University (MSU) to a more automated and high-throughput data collection platform (Bruker Avance IIITM). This instrumentation will be used by a diverse group of researchers from MSU Departments of Chemistry and Biochemistry, Veterinary Molecular Biology, Chemical and Biochemical Engineering, the Center for Biofilm Engineering, the Department of Cell Biology and Neuroscience, and the NIH Rocky Mountain Laboratory. Currently, none of the solution NMR spectrometers in the MSU Structural Biology and Chemistry NMR Facility are equipped with a cryoprobe, and the requested instrumentation and upgrade of the spectrometer console hardware will be the first of its kind on campus. The requested instrumentation upgrades will enhance sensitivity and maximize throughput of MSU 600 MHz solution NMR spectrometer. It will contribute significantly to the successful completion of challenging NMR-based structural biology projects and the expansion of NMR metabolomics research programs that are being developed on campus. The very substantially enhanced sensitivity achieved with the requested instrumentation will allow acquisition of experiments and studies on challenging biological samples, which are currently not possible because of limited sample solubility, limited sample stability, or limited instrument time availability. The console upgrade will allow automated shimming and performance optimization, and will provide much more efficient use of the recently purchased automatic sample loading system (Bruker SampleJetTM). The combination of the console upgrade and the automatic sample loading system will allow more effective 24/7 utilization of the 600 MHz NMR instrument. The cryoprobe and upgraded console will greatly facilitate the expansion of our existing NMR metabolomics capabilities (which include ChenomxTM and AMIXTM software for metabolite profiling analysis). Enhancement of NMR structural biology and metabolomics infrastructure is desired by a number of prospective users and supports the development of a new NIH-funded P20 Center for the Analysis of Cellular Mechanisms and Systems Biology. MSU's DRX 600 NMR instrument is used quite heavily, but the enhanced sensitivity and performance provided by the requested upgrades will allow this instrument to accomplish much more. The addition of the requested instrumentation will leverage significantly enhanced biomedical research capabilities for a broad group of researchers on the MSU-Bozeman campus. The requested instrumentation will also provide opportunities for new research directions in translational biomedical research, will support expanded systems biology approaches at MSU, and will contribute to the training and employment of numerous graduate students, post-doctoral fellows, and research staff.

Public Health Relevance

We request support from the NIH to enhance the nuclear magnetic resonance (NMR) biomedical research capabilities of Montana State University. The requested instrumentation will enhance the research capabilities of a broad group of scientists involved in better understanding the molecular basis of iron homeostasis, host-pathogen interactions, viral infections, Alzheimer's, diabetes, AIDS, and other important human diseases.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biomedical Research Support Shared Instrumentation Grants (S10)
Project #
1S10RR026659-01A1
Application #
8050694
Study Section
Special Emphasis Panel (ZRG1-BCMB-K (30))
Program Officer
Levy, Abraham
Project Start
2011-08-15
Project End
2013-08-14
Budget Start
2011-08-15
Budget End
2013-08-14
Support Year
1
Fiscal Year
2011
Total Cost
$600,000
Indirect Cost
Name
Montana State University - Bozeman
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
625447982
City
Bozeman
State
MT
Country
United States
Zip Code
59717
Weaver, Alan J; Peters, Tami R; Tripet, Brian et al. (2018) Exposure of Methicillin-Resistant Staphylococcus aureus to Low Levels of the Antibacterial THAM-3?G Generates a Small Colony Drug-Resistant Phenotype. Sci Rep 8:9850
Partovi, Sarah E; Mus, Florence; Gutknecht, Andrew E et al. (2018) Coenzyme M biosynthesis in bacteria involves phosphate elimination by a functionally distinct member of the aspartase/fumarase superfamily. J Biol Chem 293:5236-5246
Rawle, Rachel A; Hamerly, Timothy; Tripet, Brian P et al. (2017) Multi-omics analysis provides insight to the Ignicoccus hospitalis-Nanoarchaeum equitans association. Biochim Biophys Acta Gen Subj 1861:2218-2227
Tokmina-Lukaszewska, Monika; Shi, Zunji; Tripet, Brian et al. (2017) Metabolic response of Agrobacterium tumefaciens 5A to arsenite. Environ Microbiol 19:710-721
Hamerly, Timothy; Tripet, Brian; Wurch, Louie et al. (2015) Characterization of Fatty Acids in Crenarchaeota by GC-MS and NMR. Archaea 2015:472726
Ammons, Mary Cloud B; Morrissey, Kathryn; Tripet, Brian P et al. (2015) Biochemical association of metabolic profile and microbiome in chronic pressure ulcer wounds. PLoS One 10:e0126735
Hamerly, Timothy; Tripet, Brian P; Tigges, Michelle et al. (2015) Untargeted metabolomics studies employing NMR and LC-MS reveal metabolic coupling between Nanoarcheum equitans and its archaeal host Ignicoccus hospitalis. Metabolomics 11:895-907
Fonner, Brittany A; Tripet, Brian P; Lui, Mengyao et al. (2014) ¹H, ¹³C, ¹?N backbone and side chain NMR resonance assignments of the N-terminal NEAr iron transporter domain 1 (NEAT 1) of the hemoglobin receptor IsdB of Staphylococcus aureus. Biomol NMR Assign 8:201-5
Mason, Katelyn E; Tripet, Brian P; Parrott, David et al. (2014) ¹H, ¹³C, ¹?N backbone and side chain NMR resonance assignments for the N-terminal RNA recognition motif of the HvGR-RBP1 protein involved in the regulation of barley (Hordeum vulgare L.) senescence. Biomol NMR Assign 8:149-53
Fonner, Brittany A; Tripet, Brian P; Eilers, Brian J et al. (2014) Solution structure and molecular determinants of hemoglobin binding of the first NEAT domain of IsdB in Staphylococcus aureus. Biochemistry 53:3922-33

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