2 papers
q-bio.SC2019
How kinesin waits for ATP affects the nucleotide and load dependence of the stepping kinetics
Ryota Takaki, Mauro L. Mugnai, Yonathan Goldtzvik +1
Dimeric molecular motors walk on polar tracks by binding and hydrolyzing one ATP per step. Despite tremendous progress, the waiting state for ATP binding in the well-studied kinesi…
physics.bio-ph2015
On the importance of hydrodynamic interactions in the stepping kinetics of kinesin
Yonathan Goldtzvik, Zhechun Zhang, D. Thirumalai
Conventional kinesin walks by a hand-over-hand mechanism on the microtubule (MT) by taking 8 discrete steps, and consumes one ATP molecule per step. The time needed to c…