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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McKay, Matthew J; Martfeld, Ashley N; De Angelis, Anna A et al. (2018) Control of Transmembrane Helix Dynamics by Interfacial Tryptophan Residues. Biophys J 114:2617-2629
Radoicic, Jasmina; Park, Sang Ho; Opella, Stanley J (2018) Macrodiscs Comprising SMALPs for Oriented Sample Solid-State NMR Spectroscopy of Membrane Proteins. Biophys J 115:22-25
Dutta, Samit Kumar; Yao, Yong; Marassi, Francesca M (2017) Structural Insights into the Yersinia pestis Outer Membrane Protein Ail in Lipid Bilayers. J Phys Chem B 121:7561-7570
Berkamp, Sabrina; Park, Sang Ho; De Angelis, Anna A et al. (2017) Structure of monomeric Interleukin-8 and its interactions with the N-terminal Binding Site-I of CXCR1 by solution NMR spectroscopy. J Biomol NMR 69:111-121
Tian, Ye; Schwieters, Charles D; Opella, Stanley J et al. (2017) High quality NMR structures: a new force field with implicit water and membrane solvation for Xplor-NIH. J Biomol NMR 67:35-49
Opella, Stanley J; Marassi, Francesca M (2017) Applications of NMR to membrane proteins. Arch Biochem Biophys 628:92-101
Park, Sang Ho; Berkamp, Sabrina; Radoicic, Jasmina et al. (2017) Interaction of Monomeric Interleukin-8 with CXCR1 Mapped by Proton-Detected Fast MAS Solid-State NMR. Biophys J 113:2695-2705
Yao, Yong; Dutta, Samit Kumar; Park, Sang Ho et al. (2017) High resolution solid-state NMR spectroscopy of the Yersinia pestis outer membrane protein Ail in lipid membranes. J Biomol NMR 67:179-190
Yao, Yong; Nisan, Danielle; Fujimoto, Lynn M et al. (2016) Characterization of the membrane-inserted C-terminus of cytoprotective BCL-XL. Protein Expr Purif 122:56-63
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 262:20-26

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