A consortium of three Universities: The University of Colorado, Boulder, the University of Colorado Health Science Center (UCHSC) and the University of Utah School of Medicine will purchase an 800 MHZ NMR spectrometer with partial support from the NCRR Shared Instrumentation and NSF Multi-User Biological Instrumentation Program. This field NMR will benefit the research programs of the seven major users (A. Pardi and D.S. Wuttke at Boulder; W.L. Sundquist and D.R. Davis at Utah; and B.K. Bendiak, D.N.M Jones, and M.J. Overduin at UCHSC) and several minor users at the three institutions. Recent developments in TROSY-type experiments allow acquisition of extremely high resolution NMR spectra on much larger macromolecules than was previously possible. These TROSY experiments are optimized at ultra-high magnetic fields, and the requested 800 MHZ NMR will make it possible for the major users to take advantage of these powerful new techniques. The instrument will be housed in the basic science building that is part of the new campus currently being constructed for UCHSC in Denver. The major users currently have access to 500 and 600 MHZ NMR instrumentation so the requested 800 NMR will be used for projects that have a demonstrated need for a higher field, higher resolution and higher sensitivity of the 800 MHz spectrometer. The requested instrument will accelerate new and ongoing research projects in the following areas: - Oligosaccharide Structures and Cell Surface Carbohydrate-Protein Interactions- B.K. Bendiak - Structural Studies of HIV Primer/Template Complex-D.R. Davis - Structural Function Studies of Proteins and Carbohydrates Involved in Disease- D.N.M. Jones - Structures, Interactions and Dynamics of Membrane-Associated Proteins- M.J. Overduin - Structure-Function Studies of RNA-A. Pardi - Structural Studies of HIV-1 Assembly and Budding- W.I. Sundquist - Structural Studies of Biologically Important Molecular Recognition- D.S. Wuttke

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biomedical Research Support Shared Instrumentation Grants (S10)
Project #
1S10RR016649-01
Application #
6441010
Study Section
Special Emphasis Panel (ZRG1-PB (01))
Program Officer
Tingle, Marjorie
Project Start
2002-07-15
Project End
2005-07-14
Budget Start
2002-07-15
Budget End
2005-07-14
Support Year
1
Fiscal Year
2002
Total Cost
$500,000
Indirect Cost
Name
University of Colorado at Boulder
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
City
Boulder
State
CO
Country
United States
Zip Code
80309
Wall, Kathryn P; Hough, Loren E (2018) In-Cell NMR within Budding Yeast Reveals Cytoplasmic Masking of Hydrophobic Residues of FG Repeats. Biophys J 115:1690-1695
Warner, Lisa R; Gatzeva-Topalova, Petia Z; Doerner, Pamela A et al. (2017) Flexibility in the Periplasmic Domain of BamA Is Important for Function. Structure 25:94-106
Wall, Kathryn P; Pagratis, Maria; Armstrong, Geoffrey et al. (2016) Molecular Determinants of Tubulin's C-Terminal Tail Conformational Ensemble. ACS Chem Biol 11:2981-2990
Xiao, Yao; Warner, Lisa R; Latham, Michael P et al. (2015) Structure-Based Assignment of Ile, Leu, and Val Methyl Groups in the Active and Inactive Forms of the Mitogen-Activated Protein Kinase Extracellular Signal-Regulated Kinase 2. Biochemistry 54:4307-19
Xiao, Yao; Lee, Thomas; Latham, Michael Parker et al. (2014) Phosphorylation releases constraints to domain motion in ERK2. Proc Natl Acad Sci U S A 111:2506-11
Warner, Lisa R; Varga, Krisztina; Lange, Oliver F et al. (2011) Structure of the BamC two-domain protein obtained by Rosetta with a limited NMR data set. J Mol Biol 411:83-95
Gatzeva-Topalova, Petia Zvezdanova; Warner, Lisa Rosa; Pardi, Arthur et al. (2010) Structure and flexibility of the complete periplasmic domain of BamA: the protein insertion machine of the outer membrane. Structure 18:1492-501
Walton, Troy A; Sandoval, Cristina M; Fowler, C Andrew et al. (2009) The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains. Proc Natl Acad Sci U S A 106:1772-7
Latham, Michael P; Zimmermann, Grant R; Pardi, Arthur (2009) NMR chemical exchange as a probe for ligand-binding kinetics in a theophylline-binding RNA aptamer. J Am Chem Soc 131:5052-3
Latham, Michael P; Hanson, Paul; Brown, Darin J et al. (2008) Comparison of alignment tensors generated for native tRNA(Val) using magnetic fields and liquid crystalline media. J Biomol NMR 40:83-94

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