Abstract
One of the most important duties of a kinesin molecular motor is to not fall off its microtubule track. However, despite considerable advances in our understanding of the structure and mechanism of kinesin in recent years, we have remained mostly in the dark about what enables this motor protein to take many steps in a row before detaching—a feature known as processivity. In this issue of the Biophysical Journal, Mickolajczyk and Hancock (1) give us valuable new insight into a kinetic race in the kinesin ATPase cycle that is central to processivity in these motors.
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