The National Magnetic Resonance Facility at Madison (NMRFAM) is a resource center for biomolecular nuclear magnetic resonance (NMR) spectroscopy and small angle X-ray scattering (SAXS). 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, such as complexes, membrane proteins, paramagnetic proteins, and larger RNA molecules, and (3) efficient approaches to metabolomics, screening of small molecules binding to biological macromolecules, and natural product analysis. NMRFAM strives to be a model to the larger biological community for demonstrating 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 development projects. Through its collaborative activities, NMRFAM develops and disseminates advanced approaches that cover all steps in biomolecular NMR investigations. The center 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) preparation and labeling of proteins and nucleic acids, (3) feasibility studies, (4) data collection, (5) data analysis and structure determination, (6) data deposition, and (7) manuscript preparation. NMRFAM aims to facilitate the efficient pursuit of new knowledge by providing researchers with resources matched to their particular needs. 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. NMRFAM conducts annual workshops and group training sessions as other means for training its user base and for disseminating its novel technology. Additional mechanisms used to disseminate NMRFAM technology include newsletters, the NMRFAM website, software servers, a metabolomics database (hosted at BMRB), presentations at meetings, and the publication of articles and reviews.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Biotechnology Resource Grants (P41)
Project #
5P41GM103399-34
Application #
9645641
Study Section
Special Emphasis Panel (ZRG1)
Project Start
Project End
2021-02-28
Budget Start
2019-03-01
Budget End
2020-02-29
Support Year
34
Fiscal Year
2019
Total Cost
Indirect Cost
Name
University of Wisconsin Madison
Department
Type
DUNS #
161202122
City
Madison
State
WI
Country
United States
Zip Code
53715
Pupier, Marion; Nuzillard, Jean-Marc; Wist, Julien et al. (2018) NMReDATA, a standard to report the NMR assignment and parameters of organic compounds. Magn Reson Chem 56:703-715
Zhang, Fan; Braun, Doug R; Ananiev, Gene E et al. (2018) Biemamides A-E, Inhibitors of the TGF-? Pathway That Block the Epithelial to Mesenchymal Transition. Org Lett 20:5529-5532
Gandhi, N N; Cobra, P F; Steele, J L et al. (2018) Lactobacillus demonstrate thiol-independent metabolism of methylglyoxal: Implications toward browning prevention in Parmesan cheese. J Dairy Sci 101:968-978
Cai, Kai; Frederick, Ronnie O; Dashti, Hesam et al. (2018) Architectural Features of Human Mitochondrial Cysteine Desulfurase Complexes from Crosslinking Mass Spectrometry and Small-Angle X-Ray Scattering. Structure 26:1127-1136.e4
Travers, Timothy; López, Cesar A; Van, Que N et al. (2018) Molecular recognition of RAS/RAF complex at the membrane: Role of RAF cysteine-rich domain. Sci Rep 8:8461
Rhoads, Timothy W; Burhans, Maggie S; Chen, Vincent B et al. (2018) Caloric Restriction Engages Hepatic RNA Processing Mechanisms in Rhesus Monkeys. Cell Metab 27:677-688.e5
Cai, Kai; Frederick, Ronnie O; Tonelli, Marco et al. (2018) Interactions of iron-bound frataxin with ISCU and ferredoxin on the cysteine desulfurase complex leading to Fe-S cluster assembly. J Inorg Biochem 183:107-116
Yu, Corey H; Lee, Woonghee; Nokhrin, Sergiy et al. (2018) The Structure of Metal Binding Domain 1 of the Copper Transporter ATP7B Reveals Mechanism of a Singular Wilson Disease Mutation. Sci Rep 8:581
Pierson, Hannah E; Kaler, Mandeep; O'Grady, Christopher et al. (2018) Engineered Protein Model of the ATP synthase H+- Channel Shows No Salt Bridge at the Rotor-Stator Interface. Sci Rep 8:11361
Thomas, Nathan E; Wu, Chao; Morrison, Emma A et al. (2018) The C terminus of the bacterial multidrug transporter EmrE couples drug binding to proton release. J Biol Chem 293:19137-19147

Showing the most recent 10 out of 169 publications