What is Biophysics?
Molecular biophysics brings fundamental principles and concepts from physics, chemistry and engineering to bear on the ever-expanding menu of challenging problems in biology. The unifying theme is the quantitative analysis of biological systems of various complexities at the molecular level, using a variety of experimental, theoretical and computational methods. Dramatic advances in technology and computing power, combined with the ability to produce a host of target systems in vitro and in vivo, now enable unprecedented opportunities to unravel structure and function relationships in biological systems and understand the molecular basis of disease.
Our research in the area of Biochemistry
Research programs in the Department of Biochemistry and Molecular Pharmacology (BMP) explore molecular recognition and function in protein-protein, protein-DNA and protein-RNA complexes (Kelch, Royer, Weng Xu labs), map energy surfaces for protein folding reactions (Matthews, Bilsel, and Zitzewitz labs), probe the molecular consequences of drug resistance (Schiffer lab), understand the mechanism of toxicity for neurodegenerative diseases (Bilsel, Matthews, Massi, and Zitzewitz labs) , test hypotheses for membrane fusion and membrane transport reactions (Munson, Kobertz and Carruthers labs), develop nanoparticle tools for imaging and drug delivery (Han lab), examine the structure and dynamic properties of single molecules (Matthews, Bilsel, and Zitzewitz labs), and venture into the emerging field of molecular evolution (Zeldovich, Matthews, and Bolon labs). All of these studies are supported by a variety of technology, including crystallography, cryo-electron microscopy, NMR spectroscopy, calorimetry, fluorescence, circular dichroism and dynamic and multi-angle light scattering spectroscopy, mass spectrometry and high performance computing.
Our breakthrough discoveries
BMP researchers have made important breakthroughs in many areas of Biophysics. The Carruthers lab measured and modeled the metabolic response of the human visual cortex to light activation. The Schiffer lab has exploited the hundreds of co-crystal structures of HIV and HCV proteases with substrates and inhibitors to develop the substrate envelope theory of drug resistance. The Kelch lab played an integral role in understanding of how the clamp loader ATPase opens the clamp to load it onto DNA. The Massi lab has elucidated the molecular origin and functional effects of structural order and disorder in RNA-binding proteins. The Weng lab has developed computational algorithms for predicting protein-protein complex structures. The Matthews, Bilsel, and Zitzewitz labs have provided fundamental insights into protein folding that aid the de novo prediction of protein structures. We anticipate that the breakthrough discoveries are likely to continue at a strong pace especially given the new cryoEM facility being established under the leadership of Dr. Chen Xu.