Document Type
Article
Publication Date
7-5-2010
Publication Title
BioMed Central Structural Biology
Department
Department of Chemistry
Abstract
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.
DOI
10.1186/1472-6807-10-19
Original Citation
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.
https://digitalcommons.dartmouth.edu/facoa/2410
