Abstract
During each step taken by a dimeric kinesin motor, one motor domain must release from its previous binding site on the microtubule and move 16 nm forward to the next binding site. This stepping process is thought to involve both concerted conformational changes and diffusive movement, but the relative role played by these two processes is not clear. We are investigating this question by computationally modeling the chemomechanical cycle of kinesin using Brownian dynamics simulations. The simulations model the diffusion of the tethered kinesin head and incorporate resistive forces from the motor's flexible neck-linker domain and a distance-dependent on-rate for binding to the next site on the microtubule.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
