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 experien

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.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Biotechnology Resource Grants (P41)
Project #
5P41GM103399-33
Application #
9433640
Study Section
Special Emphasis Panel (ZRG1)
Program Officer
Krepkiy, Dmitriy
Project Start
1997-03-01
Project End
2020-02-29
Budget Start
2018-03-01
Budget End
2019-02-28
Support Year
33
Fiscal Year
2018
Total Cost
Indirect Cost
Name
University of Wisconsin Madison
Department
Biochemistry
Type
Earth Sciences/Resources
DUNS #
161202122
City
Madison
State
WI
Country
United States
Zip Code
53715
Chyan, Wen; Kilgore, Henry R; Gold, Brian et al. (2017) Electronic and Steric Optimization of Fluorogenic Probes for Biomolecular Imaging. J Org Chem 82:4297-4304
Mong, Surin K; Cochran, Frank V; Yu, Hongtao et al. (2017) Heterochiral Knottin Protein: Folding and Solution Structure. Biochemistry 56:5720-5725
Cai, Kai; Tonelli, Marco; Frederick, Ronnie O et al. (2017) Human Mitochondrial Ferredoxin 1 (FDX1) and Ferredoxin 2 (FDX2) Both Bind Cysteine Desulfurase and Donate Electrons for Iron-Sulfur Cluster Biosynthesis. Biochemistry 56:487-499
Handley, Lindsey D; Fuglestad, Brian; Stearns, Kyle et al. (2017) NMR reveals a dynamic allosteric pathway in thrombin. Sci Rep 7:39575
Warden, Meghan S; Tonelli, Marco; Cornilescu, Gabriel et al. (2017) Structure of RNA Stem Loop B from the Picornavirus Replication Platform. Biochemistry 56:2549-2557
Yu, Corey H; Yang, Nan; Bothe, Jameson et al. (2017) The metal chaperone Atox1 regulates the activity of the human copper transporter ATP7B by modulating domain dynamics. J Biol Chem 292:18169-18177
Dias, Andrew D; Elicson, Jonathan M; Murphy, William L (2017) Microcarriers with Synthetic Hydrogel Surfaces for Stem Cell Expansion. Adv Healthc Mater 6:
Vasquez, Joseph K; Tal-Gan, Yftah; Cornilescu, Gabriel et al. (2017) Simplified AIP-II Peptidomimetics Are Potent Inhibitors of Staphylococcus aureus AgrC Quorum Sensing Receptors. Chembiochem 18:413-423
Vasta, James D; Choudhary, Amit; Jensen, Katrina H et al. (2017) Prolyl 4-Hydroxylase: Substrate Isosteres in Which an (E)- or (Z)-Alkene Replaces the Prolyl Peptide Bond. Biochemistry 56:219-227
Cai, Kai; Frederick, Ronnie O; Tonelli, Marco et al. (2017) Mitochondrial Cysteine Desulfurase and ISD11 Coexpressed in Escherichia coli Yield Complex Containing Acyl Carrier Protein. ACS Chem Biol 12:918-921

Showing the most recent 10 out of 142 publications