This is the competitive renewal application for the grant that supports the Resource for NMR Molecular Imaging of Proteins at the University of California, San Diego. The Resource develops and applies NMR spectroscopy for the study of proteins in biological supramolecular structures, with most of the effort focused on developing a method for determining the three-dimensional structures of membrane proteins in phospholipid bilayers. As a P41-grant supported Research Resource, there are five components to the research program. (1) Core technological research and development is focused on solid-state NMR of proteins, and involves the development of instrumentation, largely the design and construction of new coils and probes;experimental methods, largely new pulse sequences;sample preparation starting with the expression of isotopically labeled proteins;and structure calculations. (2) Collaborative research is divided into two categories to reflect their impact on the Core. The Central Collaborations include structure determinations of the viroporins Vpu from HIV-1 and p7 from HCV, mercury transport membrane proteins with two, three, and four trans-membrane helices, filamentous bacteriophage coat proteins, and GPCRs (Gprotein coupled receptors). The studies of GPCRs are performed in the context of a Bioengineering Research Partnership, which relies on the Resource for its technology base. There are many Remote Collaborations with groups at other institutions interested in utilizing the Resource to study a wide variety of membrane proteins, ranging in complexity from antibiotic peptides to rhodopsin. (3) Service activities are in the areas of instrumentation development and access to the high field NMR spectrometers by expert users. (4) Training is performed continuously because many aspects of the technology are unique to the Resource. (5) Dissemination results from publications, the web site, and many email and telephone requests for specific information. We also work with the major vendors of NMR instrumentation to promote the spread of the technology developed at the Resource.

National Institute of Health (NIH)
National Institute of Biomedical Imaging and Bioengineering (NIBIB)
Biotechnology Resource Grants (P41)
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Special Emphasis Panel (ZRG1-BCMB-E (40))
Program Officer
Liu, Christina
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University of California San Diego
Schools of Arts and Sciences
La Jolla
United States
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Das, Bibhuti B; Opella, Stanley J (2016) Simultaneous cross polarization to (13)C and (15)N with (1)H detection at 60kHz MAS solid-state NMR. J Magn Reson 262:20-6
Young, Robert P; Caulkins, Bethany G; Borchardt, Dan et al. (2016) Solution-State (17)O Quadrupole Central-Transition NMR Spectroscopy in the Active Site of Tryptophan Synthase. Angew Chem Int Ed Engl 55:1350-4
Jaremko, Matt J; Lee, D John; Opella, Stanley J et al. (2015) Structure and Substrate Sequestration in the Pyoluteorin Type II Peptidyl Carrier Protein PltL. J Am Chem Soc 137:11546-9
Marassi, Francesca M; Ding, Yi; Schwieters, Charles D et al. (2015) Backbone structure of Yersinia pestis Ail determined in micelles by NMR-restrained simulated annealing with implicit membrane solvation. J Biomol NMR 63:59-65
Zhang, Hua; Lin, Eugene C; Das, Bibhuti B et al. (2015) Structural determination of virus protein U from HIV-1 by NMR in membrane environments. Biochim Biophys Acta 1848:3007-18
Yao, Yong; Fujimoto, Lynn M; Hirshman, Nathan et al. (2015) Conformation of BCL-XL upon Membrane Integration. J Mol Biol 427:2262-70
Opella, Stanley J (2015) Solid-state NMR and membrane proteins. J Magn Reson 253:129-37
Opella, Stanley J (2015) Relating structure and function of viral membrane-spanning miniproteins. Curr Opin Virol 12:121-5
Lewinski, Mary K; Jafari, Moein; Zhang, Hua et al. (2015) Membrane Anchoring by a C-terminal Tryptophan Enables HIV-1 Vpu to Displace Bone Marrow Stromal Antigen 2 (BST2) from Sites of Viral Assembly. J Biol Chem 290:10919-33
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

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