Michael F Brown

Michael F Brown

Professor, Chemistry and Biochemistry-Sci
Professor, Applied Mathematics - GIDP
Professor, BIO5 Institute
Member of the General Faculty
Member of the Graduate Faculty
Primary Department
Department Affiliations
Contact
(520) 621-2163

Research Interest

Michael F. Brown is Professor of Chemistry & Biochemistry at the University of Arizona. He is co-director of the Biological Physics Program and the Chemical Physics Program, and was a co-founder of the Biological Chemistry Program at the University of Arizona. He is internationally renowned for his work on the molecular basis of activation of G-protein-coupled receptors that are the targets for the majority of pharmaceuticals and medicines used by humans. The focus of his work is on biomembranes, with a particular emphasis on lipid-protein interactions in relation to potential drug targets involving membrane proteins. He is involved with investigation of the molecular basis of visual signaling involving rhodopsin. Moreover, Professor Brown is an expert in nuclear magnetic resonance (NMR) spectroscopy. His activities in the area of biomolecular NMR spectroscopy involve the devolvement and application of methods for studying the structure and dynamics of biomolecules. Michael Brown has authored over 130 original research papers, 10 book chapters, 4 book reviews, and has published more than 275 abstracts. His current H-index is 43. He numbers among his coworkers various prominent scientists worldwide. He presents his work frequently at national and international conferences, and is the recipient of a number of major awards. Professor Brown's many contributions have established him as a major voice in the area of biomembrane research and biomolecular spectroscopy. He is frequently a member of various review panels and exerts an influence on science policy at the national level. Among his accolades, he is an elected Fellow of the American Association for the Advancement of Science; American Physical Society; Japan Society for the Promotion of Science; and the Biophysical Society. He is a Fellow of the Galileo Circle of the University of Arizona. Most recently, he received the Avanti Award of the Biophysical Society. This premier honor recognizes his vast and innovative contributions to the field of membrane biophysics, and groundbreaking work in the development of NMR techniques to characterize lipid structure and dynamics. Most recently he presented the 2014 Avanti lecture of the Biophysical Society.

Publications

Williams, G. D., Beach, J. M., Dodd, S. W., & Brown, M. F. (1985). Dependence of deuterium spin-lattice relaxation rates of multilamellar phospholipid dispersions on orientational order. Journal of the American Chemical Society, 107(24), 6868-6873.

Abstract:

2H NMR studies of a homologous series of 1,2-diacyl-sn-glycero-3-phosphocholines with perdeuterated saturated chains, ranging in length from C12:0 to C16:0, have been performed with use of quadrupolar echo techniques at a resonance frequency of 55.4 MHz. Randomly oriented, multilamellar dispersions containing 50 wt % H2O in the liquid crystalline (Lα) phase have been employed. The 2H spin-lattice relaxation times (T1) and C-2H bond segmental order parameters (SCD) of each of the resolved quadrupolar splittings have been obtained from the powder-type spectra, corresponding to a random distribution of orientations, as well as from the 0°C oriented subspectra obtained by numerical deconvolution (de-Pakeing). Evidence that the spin-lattice relaxation rate profiles as a function of chain position T1-1(i) are related to the corresponding order profiles SCD(i) by a square-law functional dependence has been obtained, indicative of a contribution from relatively slow fluctuations in the local bilayer ordering to the relaxation. The results suggest that two broad classes of motions influence the 2H spin-lattice relaxation rates of lipid bilayers: rapid local motions, most likely due to bond rotational isomerizations and long-axis rotational diffusion of the lipid chains, as well as slower director fluctuations as found in other liquid crystalline mesophases. © 1985 American Chemical Society.

Brown, M. F., Milljanich, G. P., & Dratz, E. A. (1977). Proton spin lattice relaxation of retinal rod outer segment membranes and liposomes of extracted phospholipids. Proceedings of the National Academy of Sciences of the United States of America, 74(5), 1978-1982.

PMID: 266718;PMCID: PMC431056;

Brown, M. F., & Struts, A. V. (2013). Activation of rhodopsin based on solid-state NMR spectroscopy. Encyclopedia of Biophysics, 2231–2243.
Struts, A. V., Xu, X., Mallikarjunaiah, K. J., & Brown, M. F. (2013). Model-Free Spectral Density Mapping Applied to Dynamics of Rhodopsin in Solid-State NMR Spectroscopy. Biophysical Journal, 104, 41.
Molugu, T. R., Lee, S. K., Job, C., & Brown, M. F. (2015). Hydration-Modulated Collective Dynamics of Membrane Lipids are Revealed by Solid-State 2H NMR Relaxation. Biophysical Journal, 108, 77a.