We propose to establish a Rocky Mountain Regional NMR Center with a 900 MHz NMR serving a large number of Universities in the Rocky Mountain and Central Regions. The NMR Center will be situated on the new Fitzsimons campus of the University of Colorado Health Sciences Center, and will serve a productive group of NMR structural biologists in the areas of protein, nucleic acid and carbohydrate structure and function. The user group consists of 19 researchers at 8 Institutions. Space in the new Basic Research Building at Fitzsimons has been specifically designed for the unique siting requirements of a 900 MHz NMR and construction of the building is well underway. 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 fields, and the requested state-of-the-art 900 MHz NMR spectrometer and cryoprobe will make it possible for the users to take advantage of these powerful new techniques. The primary goal of the Center will be to provide routine access to the unique capabilities of the 900 MHz NMR in order to accelerate their biological and biomedical research programs. In addition to acquiring their NMR data on-site, experienced users will be able to acquire 900 MHz NMR data over the Internet with the aid of facility staff. A second major goal of the NMR Center will be to establish and maintain a Web-based collaboratorium for sharing information and expertise in a set of six """"""""focus areas."""""""" These focus areas are strengths of the user group and the collaboratorium will provide a valuable mechanism for experienced users to share their expertise with other users. The six initial focus areas for the NMR Center and Web collaboratorium are: Improved Resolution and Sensitivity for NMR Studies of Proteins; NMR Studies of Large Macromolecular Complexes; Studies of Protein and Nucleic Acid Dynamics; Improved Methods for NMR Studies of RNA and DNA; NMR Studies of Membrane Proteins; and Improved Spectral Resolution by Employing Reverse Micelles in Low Viscosity Solvents. A well designed organizational plan for administering the facility is presented which is modeled after plans at other established multi-user NMR and synchrotron facilities. Time on the 900 MHz NMR will be allocated based on written proposals which will be reviewed by a proposal review committee. NIH-funded research that requires the high field, high resolution, and unique capabilities of the 900 MHz NMR will be the highest priority for the center.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Biotechnology Resource Grants (P41)
Project #
5P41GM068928-04
Application #
7254697
Study Section
Special Emphasis Panel (ZRG1-SSS-A (40))
Program Officer
Wehrle, Janna P
Project Start
2003-07-15
Project End
2010-04-30
Budget Start
2008-05-01
Budget End
2009-04-30
Support Year
4
Fiscal Year
2008
Total Cost
$274,364
Indirect Cost
Name
University of Colorado at Boulder
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
007431505
City
Boulder
State
CO
Country
United States
Zip Code
80309
Singh, Surinder M; Bandi, Swati; Jones, David N M et al. (2017) Effect of Polysorbate 20 and Polysorbate 80 on the Higher-Order Structure of a Monoclonal Antibody and Its Fab and Fc Fragments Probed Using 2D Nuclear Magnetic Resonance Spectroscopy. J Pharm Sci 106:3486-3498
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
Holliday, Michael J; Armstrong, Geoffrey S; Eisenmesser, Elan Z (2015) Determination of the Full Catalytic Cycle among Multiple Cyclophilin Family Members and Limitations on the Application of CPMG-RD in Reversible Catalytic Systems. Biochemistry 54:5815-27
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
Eisenmesser, Elan Z; Capodagli, Glenn C; Armstrong, Geoffrey S et al. (2015) Inherent dynamics within the Crimean-Congo Hemorrhagic fever virus protease are localized to the same region as substrate interactions. Protein Sci 24:651-60
Bis, Regina L; Singh, Surinder M; Cabello-Villegas, Javier et al. (2015) Role of benzyl alcohol in the unfolding and aggregation of interferon ?-2a. J Pharm Sci 104:407-15
Kendrick, Agnieszka A; Holliday, Michael J; Isern, Nancy G et al. (2014) The dynamics of interleukin-8 and its interaction with human CXC receptor I peptide. Protein Sci 23:464-80
Holliday, Michael J; Zhang, Fengli; Isern, Nancy G et al. (2014) 1H, 13C, and 15N backbone and side chain resonance assignments of thermophilic Geobacillus kaustophilus cyclophilin-A. Biomol NMR Assign 8:23-7
Bis, Regina L; Stauffer, Tara M; Singh, Surinder M et al. (2014) High yield soluble bacterial expression and streamlined purification of recombinant human interferon ?-2a. Protein Expr Purif 99:138-46
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

Showing the most recent 10 out of 24 publications