The National Magnetic Resonance Facility at Madison (NMRFAM) is a resource for biomolecular nuclear magnetic resonance (NMR) spectroscopy. NMRFAM aims to expand the frontiers of biomolecular NMR spectroscopy through resource technology and development programs in the important areas of (1) high-throughput determination of structures and functions of smaller proteins and RNA molecules, (2) technology for investigating the structure and dynamics of challenging systems, including complexes, membrane proteins, paramagnetic proteins, and larger RNA molecules, and (3) efficient approaches to metabolomics and natural product analysis. NMRFAM strives to be a model to the larger biological community for cutting-edge capabilities of NMR spectroscopy. With the goal of broadening the scope of its scientific activities, NMRFAM hosts distinguished visiting scientists working in areas related to its research technology and development projects. NMRFAM develops and disseminates advanced approaches that cover all steps in biomolecular NMR investigations and offers start-to-finish support for biomedical NMR investigations with assistance in one or more of the following steps: (1) strategy evaluation and experiment design, (2) sample preparaton, (3) feasibility studies, (4) data collection, (5) data analysis and structure determination, (6) data validation and deposition, and (7) manuscript preparation. NMRFAM provides researchers with resources matched to their particular needs in their search for new knowledge. A major goal is to develop methods for making these investigations faster and less costly as well as applicable to larger classes of proteins and nucleic acids of importance in human health. NMRFAM provides young investigators and experienced spectroscopists access to state-of-the-art instrumentation with support for multiple modes of data collection either as service or collaborative projects. Protocols, pulse sequences, software tools, and databases developed through NMRFAM's research activities are made available to the general scientific community. Users receive hands-on training at the center. As another means for training its user base and for disseminating its novel technology, NMRFAM conducts annual workshops and group training sessions. Additional mechanisms used to disseminate NMRFAM technology include quarterly newsletters, the NMRFAM website, software servers, a metabolomics database, presentations at meetings, and the publication of articles and reviews.

Public Health Relevance

Biomolecular nuclear magnetic resonance spectroscopy is the single approach that offers the most detailed information about biomolecules in solution, the milieu in which they normally function. NMR enables the discovery of three-dimensional structure, molecular dynamics, and molecular interactions-factors that reveal how biological systems work, are impacted by genetic and environmental factors, and respond to drugs.

National Institute of Health (NIH)
National Institute of General Medical Sciences (NIGMS)
Biotechnology Resource Grants (P41)
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Special Emphasis Panel (ZRG1-BCMB-H (40))
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Friedman, Fred K
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University of Wisconsin Madison
Schools of Earth Sciences/Natur
United States
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Kim, Jin Hae; Bothe, Jameson R; Alderson, T Reid et al. (2015) Tangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies. Biochim Biophys Acta 1853:1416-28
Lee, Woonghee; Tonelli, Marco; Markley, John L (2015) NMRFAM-SPARKY: enhanced software for biomolecular NMR spectroscopy. Bioinformatics 31:1325-7
Tonelli, Marco; Eller, Chelcie H; Singarapu, Kiran K et al. (2015) Assignments of RNase A by ADAPT-NMR and enhancer. Biomol NMR Assign 9:81-8
Singh, Shanteri; Peltier-Pain, Pauline; Tonelli, Marco et al. (2014) A general NMR-based strategy for the in situ characterization of sugar-nucleotide-dependent biosynthetic pathways. Org Lett 16:3220-3
Kim, Jin Hae; Bothe, Jameson R; Frederick, Ronnie O et al. (2014) Role of IscX in iron-sulfur cluster biogenesis in Escherichia coli. J Am Chem Soc 136:7933-42
Berman, Helen M; Burley, Stephen K; Kleywegt, Gerard J et al. (2014) Response to On prompt update of literature references in the Protein Data Bank. Acta Crystallogr D Biol Crystallogr 70:2780
Kim, Jin Hae; Alderson, T Reid; Frederick, Ronnie O et al. (2014) Nucleotide-dependent interactions within a specialized Hsp70/Hsp40 complex involved in Fe-S cluster biogenesis. J Am Chem Soc 136:11586-9
Huang, Yiping; Nokhrin, Sergiy; Hassanzadeh-Ghassabeh, Gholamreza et al. (2014) Interactions between metal-binding domains modulate intracellular targeting of Cu(I)-ATPase ATP7B, as revealed by nanobody binding. J Biol Chem 289:32682-93
Alderson, T Reid; Kim, Jin Hae; Cai, Kai et al. (2014) The specialized Hsp70 (HscA) interdomain linker binds to its nucleotide-binding domain and stimulates ATP hydrolysis in both cis and trans configurations. Biochemistry 53:7148-59
Whigham, Leah D; Butz, Daniel E; Dashti, Hesam et al. (2014) Metabolic Evidence of Diminished Lipid Oxidation in Women With Polycystic Ovary Syndrome. Curr Metabolomics 2:269-278

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