Current Research

The advent of ultra high field magnets for NMR spectroscopy has opened important new avenues for understanding structure-function relationships in biological systems. Historically NMR has offered several advantages over other structural methods; it can be applied in a variety of environments, including aqueous solution and membrane phases; it can focus on particularly interesting features, such as the active site of an enzyme; and it can provide dynamic, as well as structural, information. Nevertheless, most structural applications have been limited by the dependence of NMR structural methods on data attainable only for smaller soluble biomolecules. Higher fields offer new sources of structural information that may change this situation. We are developing new NMR methodology and exploiting new, very high field, NMR facilities in order to explore this possibility. We are also exploring the use of new hyperpolarization devices to improve NMR sensitivity, particularly for monitoring the metabolic products of enzymatic reations.  Among the problems targeted for application of the new methods are ones related to how macromolecules function at the surfaces of biological membranes, how carbohydrates mediate cell-cell interactions, how proteins interact with other proteins in the course of a biological process, and how metabolic profiles can report on disease. See our group website for recent examples of research projects.

Selected Publications

Pomin, V. H. ; Sharp, J. S. ; Li, X. Y. ; Wang, L. C. ; Prestegard, J. H. Characterization of Glycosaminoglycans by N-15 NMR Spectroscopy and in Vivo Isotopic Labeling. Analytical Chemistry 2010, 82, 4078-4088.
Raman, S. ; Lange, O. F. ; Rossi, P. ; Tyka, M. ; Wang, X. ; Aramini, J. ; Liu, G. H. ; Ramelot, T. A. ; Eletsky, A. ; Szyperski, T. ; Kennedy, M. A. ; Prestegard, J. ; Montelione, G. T. ; Baker, D. NMR Structure Determination for Larger Proteins Using Backbone-Only Data. Science 2010, 327, 1014-1018.
Shapira, B. ; Prestegard, J. H. Electron-nuclear interactions as probes of domain motion in proteins. Journal of Chemical Physics 2010, 132.
Jiang, Y. ; McKinnon, T. ; Varatharajan, J. ; Glushka, J. ; Prestegard, J. H. ; Sornborger, A. T. ; Schuttler, H. B. ; Bar-Peled, M. Time-Resolved NMR: Extracting the Topology of Complex Enzyme Networks. Biophysical Journal 2010, 99, 2318-2326.
Lee, H. W. ; Wylie, G. ; Bansal, S. ; Wang, X. ; Barb, A. W. ; Macnaughtan, M. A. ; Ertekin, A. ; Montelione, G. T. ; Prestegard, J. H. Three-dimensional structure of the weakly associated protein homodimer SeR13 using RDCs and paramagnetic surface mapping. Protein Science 2010, 19, 1673-1685.
Liu, Y. Z. ; Kahn, R. A. ; Prestegard, J. H. Dynamic structure of membrane-anchored Arf center dot GTP. Nature Structural & Molecular Biology 2010, 17, 876-U128.