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Assistant Professor of Chemistry
X-Ray Crystallography and Physical Biochemistry of Motor Proteins and Their Cytoskeletal Partners
Our laboratory studies the detailed structural mechanisms employed by cytoskeletal proteins in order to 1) produce directed force along protein filaments and 2) mediate interactions with their various intra- or intermolecular protein targets. For ATP-driven molecular motors, as well as the GTP-driven G-protein family of molecular switches, conformational states are governed by the presence or absence of the nucleotide g -phosphate. An intriguing question is how such a small conformational change can be sensed by the protein and amplified, sometimes by several orders of magnitutde, in order to achieve the various cellular functions of these proteins. Our laboratory uses X-ray crystallography as its primary means of determining high resolution protein structures. In conjunction with site-directed mutagenesis, kinetics, and other biophysical techniques such as dynamic light scattering and analytical ultracentrifugation, X-ray crystallography provides one of the most powerful methods for exploring the details of protein function.
Visit the Kull Lab website
Publications
Kull, F.J., Schlicting, I., Becker, A., Kollmar, M., Manstein, D.J. & Holmes, K.C. An Alternate Conformation for MgADP-Beryllium Fluoride Bound Myosin II. In preparation.
Kollmar, M., Dürrwang, U., Kliche, W., Manstein, D.J. & Kull, F.J. (2002) Crystal structure of the motor domain of a class I myosin. EMBO Journal. submitted.
Kull, F.J. and Endow, S.A. (2002) Kinesin: switch I & II and the motor mechanism. Journal of Cell Science. In press.
Niemann, H.H., Knetsch, M.L.W., Scherer, A., Manstein, D.J. & Kull, F. J. (2001) Crystal structure of a dynamin GTPase domain in both nucleotide-free and GDP-bound forms. EMBO Journal. 20(21):5813-21.
Kliche, W., Fujita-Becker, S., Kollmar, M., Manstein, D.M. & Kull, F.J. (2000) Structure of a genetically engineered molecular motor. EMBO Journal. 20, 40-46.
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