This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The amino acid sequence of a protein encodes its three-dimensional structure, and this structure manifests itself in biological function. Using techniques that range from synthetic chemistry to biochemistry to cell biology, the Raines group is illuminating in atomic detail both the chemical basis and the biological purpose for protein structure and protein function. The efforts of the Raines group are leading to insights into the relationship between amino acid sequence and protein function (or dysfunction), as well as to the creation of novel molecules with desirable properties. This involves syntheses of small organic molecules for protein modification, protein/peptide synthesis and physical organic studies. Proton, carbon and phosphorus NMR experiments are required for characterization of these small organic molecules.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR002301-24
Application #
7954600
Study Section
Special Emphasis Panel (ZRG1-BCMB-E (40))
Project Start
2009-03-01
Project End
2010-02-28
Budget Start
2009-03-01
Budget End
2010-02-28
Support Year
24
Fiscal Year
2009
Total Cost
$5,084
Indirect Cost
Name
University of Wisconsin Madison
Department
Biochemistry
Type
Schools of Earth Sciences/Natur
DUNS #
161202122
City
Madison
State
WI
Country
United States
Zip Code
53715
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Xia, Youlin; Rossi, Paolo; Tonelli, Marco et al. (2017) Optimization of 1H decoupling eliminates sideband artifacts in 3D TROSY-based triple resonance experiments. J Biomol NMR 69:45-52
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