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

Siminovitch, D. J., Rance, M., Jeffrey, K. R., & Brown, M. F. (1984). The quadrupolar spectrum of a spin I = 1 in a lipid bilayer in the presence of paramagnetic ions. Journal of Magnetic Resonance, 58(1), 62-75.

Abstract:

The NMR signal from selectively deuterated molecules in a lipid bilayer where there are paramagnetic ions present in the aqueous region is influenced by both the nuclear quadrupole interaction and the dipolar interaction between the deuterium nuclei and the surrounding ions. The quadrupolar split powder pattern is no longer symmetric about the center of the spectrum. The spectra which result from the use of the quadrupole echo pulse sequence are quite complex since this sequence does not refocus the dephasing due to the dipolar interaction. A new pulse sequence which refocuses both the dipolar and quadrupolar interactions is suggested. Both 2H and 14N spectra from lipid molecules with the phosphatidylcholine headgroup obtained with the conventional quadrupole echo sequence and the new sequence are compared with predictions of density matrix theory calculations. There is excellent agreement between the experimental and simulated spectra. © 1984.

Xu, X., Struts, A. V., Giri, A. K., Mologu, T. R., Guruge, C., Faylough, S., Nascimento, C. L., Nesnas, N., Hruby, V. J., & Brown, M. F. (2017). Dynamics of Membrane Proteins Studied by Solid State 2H NMR Relaxation. Biophysical Journal.
Sefcik, M. D., Schaefer, J., Stejskal, E. O., McKay, R. A., Ellena, J. F., Dodd, S. W., & Brown, M. F. (1983). Lipid bilayer dynamics and rhodopsin-lipid interactions: New approach using high-resolution solid-state 13C NMR. Biochemical and Biophysical Research Communications, 114(3), 1048-1055.

PMID: 6615501;Abstract:

High-resolution, solid-state 13C NMR spectra have been obtained for unsonicated multilamellar dispersions of 1,2-dilauryl-sn-glycero-3-phosphocholine (DLPC), recombinant membranes containing DLPC and rhodopsin, and native retinal rod disk membranes. The roles of 1H dipolar decoupling, 1H-13C cross-polarization, and magic-angle sample spinning have been investigated. Rotating-frame 13C relaxation times have been measured and are discussed in terms of lipid bilayer dynamics and rhodopsin-lipid interactions. © 1983.

Alves, I. D., Salgado, G. F., Salamon, Z., Brown, M. F., Tollin, G., & Hruby, V. J. (2005). Phosphatidylethanolamine Enhances Rhodopsin Photoactivation and Transducin Binding in a Solid-Supported Lipid Bilayer as Determined Using Plasmon-Waveguide Resonance Spectroscopy. Biophysical Journal, 88, 198–210.
Molugu, T. R., Lee, S., & Brown, M. F. (2017). Concepts and Methods of Deuterium NMR Spectroscopy Applied to Biomembranes. Chemical Reviews.