The Lizzadro Magnetic Resonance Research Center operates seven different nuclear magnetic resonance (NMR) spectrometers at Notre Dame. Shahriar Mobashery's research group accomplished this breakthrough work using the largest field (800 MHz) instrument in this Center.
Chemical structure is directly relevant to the understanding of biology, as evidenced by the determination, using X-ray crystallography, that DNA is a double helix. Over the past decade, NMR spectroscopy has emerged as an alternative to X-ray crystallography for the determination of complex biological structure, and especially for biological structure that engages membranes. An outstanding example of the power of NMR spectroscopy to solve difficult biological structure is the solution of the structure of the “anchor” peptide domain of a bacterial membrane protein, recently accomplished here by the Mobashery group.
The protein studied is a target of the penicillin antibiotics. The structure of its anchor domain is important because this domain is used, by an as yet undetermined mechanism, to localize the protein within the bacterium so as to enable its proper participation in bacterial growth. From analysis of extensive two-dimensional NMR data, obtained on the high field NMR instrument of Lizzadro Center, the three-dimensional folded structure of this domain was solved. As the first determination of such a structure, this study provides the reference point for future evaluation of the role the membrane environment in modulating the anchor domain structure.This study was reported in the Journal of the American Chemical Society (Vol. 132, Issue 12, p. 4110).
The NMR facility is crucial to research at Notre Dame. This same instrument also contributed to a successful study completed by Jeff Peng, associate professor of chemistry and biochemistry.
In the photo:
Mobashery group with the 800 MHz spectrometer from left to right are: Jed Fisher, Qicun Shi, Weilie Zhang, Jaroslav Zajicek, Peter O'Daniel and Shahriar Mobashery.