The improvement of RF sample probes is crucial to the development of high field biological solid state NMR. Unlike solution NMR, solid state NMR techniques require exposing the delicate biological sample to very high intensity radio frequency (RF) magnetic fields. Unless the electric field component E of these fields is minimized, the sample will very likely be heated to destruction before the experiment is completed. In Core B, we will apply the """"""""low-E"""""""" technology that we have developed for double frequency widebore NMR to the important areas of triple resonance and more accessible standard bore magnets. We will also adapt these probes for the sample/flow applications that are a centerpiece of the proposal. The technology developed in this Core will not only be needed to carry out the scientific program described in the proposal, but it will broadly impact the ability of NMR spectroscopists to conduct protein structure and dynamics studies in the solid state. Any area of health and medicine that benefits from a better understanding of proteins may be affected.

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Program Projects (P01)
Project #
5P01AI074805-02
Application #
8116481
Study Section
Special Emphasis Panel (ZAI1)
Project Start
Project End
Budget Start
2010-08-01
Budget End
2011-07-31
Support Year
2
Fiscal Year
2010
Total Cost
$143,579
Indirect Cost
Name
Florida State University
Department
Type
DUNS #
790877419
City
Tallahassee
State
FL
Country
United States
Zip Code
32306
Martinot, Amanda J; Farrow, Mary; Bai, Lu et al. (2016) Mycobacterial Metabolic Syndrome: LprG and Rv1410 Regulate Triacylglyceride Levels, Growth Rate and Virulence in Mycobacterium tuberculosis. PLoS Pathog 12:e1005351
Wright, Anna K; Batsomboon, Paratchata; Dai, Jian et al. (2016) Differential Binding of Rimantadine Enantiomers to Influenza A M2 Proton Channel. J Am Chem Soc 138:1506-9
Sun, Jim; Siroy, Axel; Lokareddy, Ravi K et al. (2015) The tuberculosis necrotizing toxin kills macrophages by hydrolyzing NAD. Nat Struct Mol Biol 22:672-8
Opella, Stanley J (2015) Solid-state NMR and membrane proteins. J Magn Reson 253:129-37
Gong, Xiao-Min; Ding, Yi; Yu, Jinghua et al. (2015) Structure of the Na,K-ATPase regulatory protein FXYD2b in micelles: implications for membrane-water interfacial arginines. Biochim Biophys Acta 1848:299-306
Danilchanka, Olga; Pires, David; Anes, Elsa et al. (2015) The Mycobacterium tuberculosis outer membrane channel protein CpnT confers susceptibility to toxic molecules. Antimicrob Agents Chemother 59:2328-36
Opella, Stanley J (2015) Relating structure and function of viral membrane-spanning miniproteins. Curr Opin Virol 12:121-5
Speer, Alexander; Sun, Jim; Danilchanka, Olga et al. (2015) Surface hydrolysis of sphingomyelin by the outer membrane protein Rv0888 supports replication of Mycobacterium tuberculosis in macrophages. Mol Microbiol 97:881-97
Neyrolles, Olivier; Wolschendorf, Frank; Mitra, Avishek et al. (2015) Mycobacteria, metals, and the macrophage. Immunol Rev 264:249-63
Das, Nabanita; Dai, Jian; Hung, Ivan et al. (2015) Structure of CrgA, a cell division structural and regulatory protein from Mycobacterium tuberculosis, in lipid bilayers. Proc Natl Acad Sci U S A 112:E119-26

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