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

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.
Brown, M. F., Thurmond, R. L., Dodd, S. W., Otten, D., & Beyer, K. (2001). Composite membrane deformation on the mesoscopic length scale. Physical Review E - Statistical, Nonlinear, and Soft Matter Physics, 64(1 I), 010901/1-010901/4.

Abstract:

Nuclear magnetoresistance (NMR) studies were carried out to investigate a series of phospholipids in the Lα state. The influences of the acyl length, lipid polar head groups, addition of a cosurfactant, and incorporation of cholesterol were determined in terms of the bilayer viscoelastic properties. The results imply that the concept of elastic deformation of membranes is applicable on the mesoscopic length scale, approaching the molecular dimensions, with quasicoherent nodes on the order of the bilayer hydrocarbon thickness and less.

Leioatts, N., Mertz, B., Martínez-Mayorga, K., Romo, T. D., Pitman, M. C., Feller, S. E., Grossfield, A., & Brown, M. F. (2014). Retinal Makes Concerted Conformational Changes During Early Stages of Rhodopsin Activation. Biophysical Journal, 106, 54a.
Lamparski, H., Liman, U., Barry, J. A., Frankel, D. A., Ramaswami, V., Brown, M. F., & O'Brien, D. F. (1992). Photoinduced destabilization of liposomes. Biochemistry, 31(3), 685-694.

PMID: 1731924;Abstract:

The stability of two-component liposomes composed of the polymerizable 1,2-bis-[10-(2′,4′-hexadienoyloxy)decanoyl]-sn-glycero-3- phosphatidylcholine (SorbPC) and either a phosphatidylethanolamine (PE) or a phosphatidylcholine (PC) were examined via fluorescence leakage assays. Ultraviolet light exposure of SorbPC-containing liposomes forms poly-SorbPC, which phase separates from the remaining monomeric lipids. If the nonpolymerizable lipids are PE's, then the photoinduced polymerization destabilizes the liposome with loss of aqueous contents. The permeability of the control dioleoylPC/SorbPC membranes was not affected by photopolymerization of SorbPC. The photodestabilization of dioleoylPE/SorbPC (3:1) liposomes required the presence of oligolamellar liposomes. NMR spectroscopy of extended bilayers of dioleoylPE/SorbPC (3:1) showed that the photopolymerization lowers the temperature for the appearance of 31P NMR signals due to the formation of isotropically symmetric lipid structures. These observations suggest the following model for the photoinduced destabilization of liposomes composed of PE/SorbPC: photopolymerization induced phase separation with the formation of enriched domains of PE, which allows the close approach of apposed regions of enriched PE lamellae and permits the formation of an isotropically symmetric structure between the lamellae. The formation of such an interlamellar attachment (ILA) between the lamellae of an oligolamellar liposome provides a permeability pathway for the light-stimulated leakage of entrapped water-soluble reagents. © 1992 American Chemical Society.