In the most general sense, we aim to understand how proteins function in important biological processes by determining their structures at atomic resolution and by using complementary biochemical and biological experiments. The primary approach we employ is X-ray crystallography. As appropriate, we also utilize other structural methods such as nuclear magnetic resonance and electron microscopy, physical approaches such as analytical ultracentrifugation, surface Plasmon resonance, fluorescence anisotropy, and isothermal calorimetry, and the methods of protein biochemistry and proteomics. Many of our projects are collaborative and include yeast genetic or mammalian cell culture experiments that relate structural features to phenotype.
Proteasome Activation
The proteasome performs most of the proteolysis that occurs in the eukaryotic cytosol and nucleus, and is required for many (perhaps most) facets of cellular function.
moreNucleosome Remodeling
and Reorganization
Remodeling and reorganization of nucleosome structure is critically important for the regulation of replication and transcription.
moreHIV Biology
Important questions in HIV biology include understanding the interactions with cellular components that facilitate or oppose viral replication.
moreOther Collaborative Projects
We collaborate with various investigators at the University of Utah to advance understanding of diverse biological areas. These include structural aspects of isoprene biosynthesis with Dale Poulter and molecular recognition in the visual system with Wolfgang Baehr.
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