Michael F Brown
Professor, Applied Mathematics - GIDP
Professor, BIO5 Institute
Professor, Chemistry and Biochemistry-Sci
Primary Department
(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

Shrestha, U., Bhowmik, D., Perera, S. M., Chawla, U., Struts, A. V., Graziano, V., Qian, S., Heller, W. T., Brown, M. F., & Chu, X. Q. (2015). Small Angle Neutron and X-Ray Scattering Reveal Conformational Differences in Detergents Affecting Rhodopsin Activation. Biophysical Journal, 108, 39a.
Struts, A. V., Barmasov, A. V., & Brown, M. F. (2015). Spectral Methods for Study of the G-Protein-Coupled Receptor Rhodopsin. I. Vibrational and Electronic Spectroscopy. Optics and Spectroscopy, 711-717.
Schroeder, T. P., Job, C., Brown, M. F., Glass, R. S., You, N., & Block, E. (1997). 1H-{125Te} Indirect Detection in Nuclear Magnetic Resonance Spectra of Organotellurium Compounds. Magnetic Resonance in Chemistry, 35, 752-756.
Brown, M. F. (2014). Conformational Fluctuations in G-Protein-Coupled Receptors. Bulletin of the American Physical Society, 59.
Brown, M. F., & Seelig, J. (1978). Influence of cholesterol on the polar region of phosphatidylcholine and phosphatidylethanolamine bilayers. Biochemistry, 17(2), 381-384.

PMID: 619997;Abstract:

The structural changes in the polar head group region of unsonicated bilayer membranes of 1,2-dipalmitoyl-sn-glycero-3-phosphocholine and 1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine produced by addition of cholesterol have been determined using deuterium and phosphorus-31 NMR. Incorporation of up to 50 mol % cholesterol produces little change in the phosphorus-31 chemical shielding anisotropies, compared with the values in pure bilayers above the phase transition temperatures, while some of the deuterium quadrupole splittings are reduced by almost a factor of two. Adjustment of the head group torsion angles by only a few degrees accounts for the observed spectral changes. Addition of cholesterol therefore has opposite effects on the hydrocarbon and polar regions of membranes: although cholesterol makes the hydrocarbon region gel-like, with an increased probability of trans conformations, the conformation of the polar head groups is very similar to that found in the liquid crystalline phase of pure phospholipid bilayers. © 1978 American Chemical Society.