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Our laboratory uses biophysical techniques to study protein structure and function. Our primary tool is X-ray crystallography, but we supplement this powerful technique with site-directed mutagenesis, steady state and pre-steady state kinetics, isothermal titration calorimetry, dynamic light scattering and analytical ultracentrifugation. Our goal is to understand at a fundamental level the conformational changes that occur in proteins as they complete the various cellular functions. Armed with this knowledge, we then apply our fundamental understanding of structure/function relationships in order to address the issues of molecular disease. There are currently two major areas of research in the laboratory:
Sharyn A. Endow, F. Jon Kull and Honglei Liu. (2010) “Kinesins at a glance.” Journal of Cell Science. Oct 15;123(Pt 20):3420-4. PMID: 20930137.
Yu Cheng Zhao, F. Jon Kull, Jared C. Cochran. “Modulation of the kinesin ATPase cycle by neck linker docking and microtubule binding.” Journal of Biological Chemistry. Aug 13;285(33):25213-20. PMCID: PMC2919084.
Elisabeth Heuston, C. Eric Bronner, F. Jon Kull and Sharyn A Endow. (2010) “A kinesin motor in a force-producing conformation.” BMC Structural Biology. Jul 5;10:19. PMCID: PMC2906495.
Lowden, M.J., K. Skorupski, M. Pellegrini, M.G. Chiorazzo, R.K. Taylor, and F.J. Kull. (2010) Structure of Vibrio cholerae ToxT reveals a mechanism for fatty acid regulation of virulence genes. Proc. Natl. Acad. Sci. USA. Feb 16;107(7):2860-5. PMCID: PMC284031.