Understanding how any motor works requires specifying the motor's mechanical components and determining how these components move and interact during the force-generating process. The internal workings of motor proteins, which power muscle contraction, propel swimming sperm, and carry organelles along tracks in cells, are not understood. This proposal intends to reveal the mechanical elastic components of the motor protein kinesin.
The specific aims are: to measure the elasticity of kinesin under (1) torsional, (2) longitudinal, and (3) extensional forces, to locate the corresponding molecular compliant elements, and to evaluate the impact of these external forces on kinesin force generation. Optical tweezers and calibrated force fibers will be used to measure force and displacement of single-molecules for the characterization of motor elastic properties. Recombinant protein expression techniques will be utilized to identify the elastic components. The information obtained in this proposal can be used to develop a model for operation of the kinesin machine.

Agency
National Institute of Health (NIH)
Institute
National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIAMS)
Type
Postdoctoral Individual National Research Service Award (F32)
Project #
5F32AR008558-02
Application #
6171791
Study Section
Molecular and Cellular Biophysics Study Section (BBCA)
Program Officer
Lymn, Richard W
Project Start
2000-09-30
Project End
Budget Start
2000-09-30
Budget End
2001-09-29
Support Year
2
Fiscal Year
2000
Total Cost
$32,416
Indirect Cost
Name
University of Washington
Department
Physiology
Type
Schools of Medicine
DUNS #
135646524
City
Seattle
State
WA
Country
United States
Zip Code
98195
Schief, William R; Clark, Rutilio H; Crevenna, Alvaro H et al. (2004) Inhibition of kinesin motility by ADP and phosphate supports a hand-over-hand mechanism. Proc Natl Acad Sci U S A 101:1183-8
Bradley, Philip; Chivian, Dylan; Meiler, Jens et al. (2003) Rosetta predictions in CASP5: successes, failures, and prospects for complete automation. Proteins 53 Suppl 6:457-68