BioMed Central Structural Biology
Department of Chemistry
Kinesin motors hydrolyze ATP to produce force and move along microtubules, converting chemical energy into work by a mechanism that is only poorly understood. Key transitions and intermediate states in the process are still structurally uncharacterized, and remain outstanding questions in the field. Perturbing the motor by introducing point mutations could stabilize transitional or unstable states, providing critical information about these rarer states.
Heuston E, Bronner CE, Kull FJ, Endow SA. A kinesin motor in a force-producing conformation. BMC Struct Biol. 2010 Jul 5;10:19. doi: 10.1186/1472-6807-10-19. PMID: 20602775; PMCID: PMC2906495.
Dartmouth Digital Commons Citation
Heuston, Elisabeth; Bronner, C. Eric; Kull, F Jon; and Endow, Sharyn A., "A Kinesin Motor in a Force-Producing Conformation" (2010). Dartmouth Scholarship. 2410.