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

Brown, M. F., & Schleich, T. (1975). Circular dichroism and gel filtration behavior of subtilisin enzymes in concentrated solutions of guanidine hydrochloride. Biochemistry, 14(14), 3069-3074.

PMID: 238582;Abstract:

The circular dichroism of diisopropylphosphorylsubtilisins Novo and Carlsberg in both the near- and farultraviolet spectral regions is unaltered by concentrations of guanidine hydrochloride as high as 4 M at neutral pH. At concentrations of guanidine hydrochloride greater than 4 M slow irreversible time-dependent changes, apparently obeying second-order kinetics, are evident in both the near- and far-ultraviolet circular dichroism of these enzymes. Gel filtration studies of inactivated subtilisin enzymes reveal the circular dichroism changes to be accompanied by the ap-pearance of aggregated protein material. The changes in circular dichroism and the production of associated subtilisin species are sensitive to protein concentration, denaturant concentrations, and pH. The circular dichroism of active subtilisins Novo and Carlsberg in guanidine hydrochloride exhibits irreversible changes similar to those observed for the inactivated subtilisins. Aggregated protein material is also formed initially in the presence of guanidine hydrochloride, but is rapidly autolyzed to low molecular weight fragments.

Tanaka, K., Struts, A. V., Krane, S., Fujioka, N., F., G., Martínez-Mayorga, K., Brown, M. F., & Nakanishi, K. (2007). Synthesis of CD3-labeled 11-cis-retinals and application to solid-state deuterium NMR spectroscopy of rhodopsin. Bulletin of the Chemical Society of Japan, 80(11), 2177-2184.

Abstract:

Efficient synthesis of 11-Z-retinals labeled with 2H at the C5, C9, or C13 methyl groups is described. The 2H-labeled retinals were used to regenerate the visual pigment rhodopsin for structural investigations. Solid-state 2H NMR data provided the orientation of retinal within the rhodopsin binding pocket as well as its conformation. Extension of the approach to other membrane receptors can yield knowledge of their mechanisms of activation as a guide for ligand-based drug design. © 2007 The Chemical Society of Japan.

Ying, J., Ahn, J. M., Jacobsen, N. E., Brown, M. F., & Hruby, V. J. (2003). NMR Solution Structure of the Glucagon Antagonist [desHis1, desPhe6, Glu9]Glucagon Amide in the Presence of Perdeuterated Dodecylphosphocholine Micelles. Biochemistry, 42, 2825-2835.
Brown, M. F. (2012). Curvature Forces in Membrane Lipid-Protein Interactions. Bulletin of the American Physical Society, 57.
Salamon, Z., Wang, Y., Brown, M. F., MacLeod, A., & Tollin, G. (1994). Conformational Changes in Rhodopsin Probed by Surface Plasmon Resonance Spectroscopy. Biochemistry, 33, 13706-13711.