个人简介

Avanti Award of the Biophysical Society, 2014 Biophysical Society Fellow,, 2013 Fellow of American Association for the Advancement of Science, 2012 American Physical Society Fellow, 2011 NIH Research Career Development Award, 1985-90 Alfr

研究领域

Biochemistry/Physical/Bioanalytical/Biophysics/Chemical Biology/Chemical Physics/Instrument Development/Protein and Membrane Biochemistry/Spectroscopy/molecular Structure/Structural Biology/Surfaces an

Our research team is committed to discovering new knowledge at the cutting edge of molecular spectroscopy and biophysical chemistry. In the area of spectroscopy and analytical methods, we apply nuclear magnetic resonance (NMR) technologies to liquid-crystalline materials and biomolecular systems. NMR spectroscopy is perhaps the most useful analytical method in chemistry and biochemistry. It provides information about both structure and dynamics, with amazing breadth and versatility. Applications range from organic synthesis to protein structure elucidation, studies of membranes and (bio)polymers, and magnetic resonance imaging (MRI) of human subjects. Currently my students are applying solid-state NMR spectroscopy to membrane liquid crystals and proteins. We study membrane lipids and membrane proteins using solution and solid-state NMR methods. Moreover, our group uses solid-state NMR to investigate small molecule cofactors bound to membrane proteins. In the area of biophysical chemistry, our laboratory is engaged in studies of proteolipid membranes. Chemical, physical, analytical, and biochemical methods provide opportunities for cross-disciplinary training. Members of our team conduct research at US National Laboratories (Oak Ridge, Brookhaven, SLAC), where X-rays and neutrons are used to investigate molecular structure and dynamics. New directions entail femtosecond X-ray crystallography with a free electron laser to investigate conformational changes of membrane proteins. Establishing how proteins like rhodopsin are affected by lipid bilayer deformation is another important emphasis of our multidisciplinary group.

近期论文

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Kinnun, J. J., Mallikarjunaiah, K. J., Petrache, H. I., and Brown, M. F. (2015), Elastic Deformation and Area Per Lipid of Membranes: Atomistic View From Solid-State Deuterium NMR Spectroscopy, Biochim. Biophys. Acta 1848, 246-259. Struts, A. V., Chawla, U., Perera, S. M. D. C., and Brown, M. F. (2015), Investigation of Rhodopsin Dynamics in its Signaling State by Solid-State Deuterium NMR Spectroscopy, in Methods in Molecular Biology, Jastrzebska, B. (Ed.), Springer, in press. Leftin, A., Molugu, T. R., Job, C., Beyer, K., Brown, M. F. (2014), Area per lipid and cholesterol interactions in membranes from separated local-field 13C NMR spectroscopy, Biophys. J. 107, 2274-2286. Leioatts, N., Mertz, B., Mart�nez-Mayorga, K., Romo, T. D., Pitman, M. C., Feller, S. E., Grossfield, A., and Brown, M. F. (2014), Retinal ligand mobility explains internal hydration and reconciles active rhodopsin structures, Biochemistry 53, 376-385. Xu, X., Struts, A. V., and Brown, M. F. (2014), Generalized Model-Free Analysis of Nuclear Spin Relaxation Experiments, eMagRes 3, 275-286. Struts, A. V., and Brown, M. F. (2014), Structural Dynamics of Retinal in Rhodopsin Activation Viewed by Solid-State 2H NMR Spectroscopy, in Advances in Biological Solid-State NMR: Proteins and Membrane-Active Peptides, Separovic, F., and Naito, A. (Eds.), The Royal Society of Chemistry, Cambridge, pp. 320-352. Zhu, S., Brown, M. F., Feller, S. E. (2013), Retinal Conformation Governs pKa of Protonated Schiff Base in Rhodopsin Activation, J. Am. Chem. Soc. 135, 9391-9398. Leftin, A., Job, C., Beyer, K., and Brown, M. F. (2013), Solid-state 13C NMR Reveals Annealing of Raft-Like Membranes Containing Cholesterol by the Intrinsically Disordered Protein α-Synuclein, J. Mol. Biol. 425, 2973-2987. Kinnun, J. J., Leftin, A., and Brown, M. F. (2013), Solid-State NMR Spectroscopy for the Undergraduate Physical Chemistry Laboratory, J. Chem. Ed. 90, 123-128. Brown, M. F. (2012), Curvature Forces in Membrane Lipid-Protein Interactions, Biochemistry 51, 9782-9795. Mertz, B., Struts, A. V., Feller, S. E., and Brown, M. F. (2012), Molecular Simulations and Solid-State NMR Investigate Dynamical Structure in Rhodopsin Activation, Biochim. Biophys. Acta 1818, 241-251. Struts, A. V., Salgado, G. F. J., Mart�nez-Mayorga, K., and Brown, M. F. (2011), Retinal dynamics underlie its switch from inverse agonist to agonist during rhodopsin activation, Nature Struct. Mol. Biol. 18, 392-394. Struts, A. V., Salgado, G. F. J., and Brown, M. F. (2011), Solid-State 2H NMR Relaxation Illuminates Functional Dynamics of Retinal Cofactor in Membrane Activation of Rhodopsin, Proc. Natl. Acad. Sci. U.S.A. 108, 8263-8268. Leftin, A., and Brown, M. F. (2011), An NMR Data Base for Simulations of Membrane Dynamics, Biochim. Biophys. Acta 1808, 818-839. Mallikarjunaiah, K. J., Leftin, A., Kinnun, J. J., Justice, M. J., Rogozea, A. L., Petrache, H. I., and Brown, M. F. (2011), Solid-State 2H NMR Demonstrates Correspondence of Hydrostatic and Osmotic Pressures in Lipid Membrane Deformation, Biophys. J. 100, 98-107.