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 major aims of the Center for Eukaryotic Structural Genomics are the development and critical analysis of methods for high-throughput, proteome-scale, eukaryotic protein production, characterization, and structure determination. This technology is being tested and refined through the determination of crystal and solution state three-dimensional structures of proteins from Arabidopsis thaliana. Particular emphasis is placed on proteins whose sequences suggest that they may contain a novel fold, proteins associated with novel functions, or proteins likely to have a known fold but with a function not previously associated with that fold. It is envisioned that most of the structures will be determined by X-ray crystallography, with NMR used for smaller, more dynamic proteins and for smaller protein targets that fail to crystallize. This work attempts to screen Arabidopsis proteins for their biologically relevent cofactors. 15N labeled proteins are allowed to mix with a library of possible cofactors, and HSQC spectra are monintered for positive interactions.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
2P41RR002301-21A1
Application #
7420572
Study Section
Special Emphasis Panel (ZRG1-BCMB-E (40))
Project Start
2006-04-20
Project End
2007-02-28
Budget Start
2006-04-20
Budget End
2007-02-28
Support Year
21
Fiscal Year
2006
Total Cost
$6,555
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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