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There is now a CONTENT FREEZE for Mercury while we switch to a new platform. It began on Friday, March 10 at 6pm and will end on Wednesday, March 15 at noon. No new content can be created during this time, but all material in the system as of the beginning of the freeze will be migrated to the new platform, including users and groups. Functionally the new site is identical to the old one. webteam@gatech.edu
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The motor protein kinesin uses adenosine triphosphate (ATP) as a fuel and walks along the microtubule filaments in the cell. They are vital for many
cellular processes including intracellular transport and cell division. Although recent progress in experiments yielded much information regarding
their motility, a structure-based, physical mechanism by which the motor amplifies the ATP-driven small conformational change in the motor head into
a large, 8-nm stepping motion remains largely a mystery. I will discuss molecular dynamics simulations elucidating its force-generation mechanism
and tests by single-molecule optical trap measurements. We find that the motion consists of autonomous force-generation and guided diffusion, where
the partitioning of the two depends on functional needs of different kinesin families.
