Adenosine Triphosphate; Biochemistry; Biophysics; Kinesin; Crystallography, X-Ray; Cryoelectron Microscopy
My more recent work has turned towards advancing cryo-electron microscopy techniques to the point where atomic-level features can be obtained for systems such as cytoskeletal filaments. These efforts led to my recent synthesis, using cryo-electron microscopy (cryo-EM) and X-ray crystallography information, of an atomic-level model for kinesin’s ATP-sensing machinery in its active form, which is only assumed following microtubule attachment. This discovery led to a simple and intuitive “seesaw” mechanism describing how ATP binding leads to force generation in the microtubule-attached motor. My laboratory's research interests are rapidly expanding to include numerous other filament-related molecular machines, such the myosin molecular motor that powers muscle movement, and diverse protein machinery involved in DNA repair and splicing.
- C. Sindelar; N. Grigorieff. An adaptation of the Wiener filter suitable for analyzing images of isolated single particles. J. Struct. Biol. 176:60-74 (2011).
- C. Sindelar. A seesaw model for intermolecular gating in the kinesin motor protein. Biophysical Reviews 3:85-100 (2011).
- Sindelar*; K. Downing. An atomic-level mechanism for activation of the kinesin molecular motors. PNAS 107:4111-4116 (2010).
- Cochran; C. Sindelar; N. Mulko; K. Collins; S. Kong; R. Hawley; F. J. Kull. ATPase Cycle of the Nonmotile Kinesin NOD Allows Microtubule End Tracking and Drives Chromosome Movement. Cell 136(1):110-22 (2009).
- C. Sindelar; K. Downing. The Beginning of Kinesin’s Force-Generating Cycle Visualized at 9 Å Resolution. J. Cell. Biol. 177(3): 377-85 (2007).