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

Wiedmann, T. S., Pates, R. D., Beach, J. M., Salmon, A., & Brown, M. F. (1988). Lipid-protein interactions mediate the photochemical function of rhodopsin. Biochemistry, 27(17), 6469-6474.

PMID: 3219348;Abstract:

We have investigated the molecular features of recombinant membranes that are necessary for the photochemical function of rhodopsin. The magnitude of the metarhodopsin I to metarhodopsin II phototransient following a 25% ± 3% bleaching flash was used as a criterion of photochemical activity at 28°C and pH 7.0. Nativelike activity of rhodopsin can be reconstituted with an extract of total lipids from rod outer segment membranes, demonstrating that the protein is minimally perturbed by the reconstitution protocol. Rhodopsin photochemical activity is enhanced by phosphatidylethanolamine head groups and docosahexaenoyl (22:6ω3) acyl chains. An equimolar mixture of phosphatidylethanolamine and phosphatidylcholine containing 50 mol % docosahexaenoyl chains results in optimal photochemical function. These results suggest the importance of both the head-group and acyl chain composition of the rod outer segment lipids in the visual process. The extracted rod lipids and those lipid mixtures favoring the conformational change from metarhodopsin I to II can undergo lamellar (Lα) to inverted hexagonal (HII) phase transitions near physiological temperature. Interaction of rhodopsin with membrane lipids close to a Lα to HII (or cubic) phase boundary may thus lead to properties which influence the energetics of conformational states of the protein linked to visual function. © 1988 American Chemical Society.

Brown, M. F., Ellena, J. F., Trindle, C., & Williams, G. D. (1985). Frequency dependence of spin-lattice relaxation times of lipid bilayers. The Journal of Chemical Physics, 84(1), 465-470.

Abstract:

2H and 13C spin-lattice (T1) relaxation time studies of 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) in the lamellar, liquid crystalline (Lα) phase are discussed. It is shown that the T1-1 results as a function of Larmor frequency ω0 are statistically better described by an ω0-1/2 dependence than by an ω 0-1 or ω0-2 dependence. © 1985 American Institute of Physics.

Perera, S. M., Shresta, U., Bhowmik, D., Struts, A. V., Chu, X., & Brown, M. F. (2016). Neutron Scattering Reveals Protein Fluctuations in GPCR Activation. Biophysical Journal, 110, 228a-229a.
Perera, S. M., Xu, X., Struts, A. V., Chawla, U., Boutet, S., Carbajo, S., Seaberg, M. D., Hunter, M. S., Martin-Garcia, J. M., Coe, J. D., Wiedorn, M. O., Nelson, G., Chamberlain, S., Deponte, D. P., Fromme, R., Grant, T. D., Kirian, R. A., Fromme, P., & Brown, M. F. (2017). Time-Resolved Wide-Angle X-ray Scattering Reveals Protein Quake in Rhodopsin Activation. Biophysical Journal.
Mallikarjunaiah, K. J., Palacio, L. A., Petrache, H. I., Kinnun, J. J., & Brown, M. F. (2014). Intermembrane Forces and Membrane Deformation Observed via Dehydration and Osmotic Pressure. Biophysical Journal, 106, 287a.