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Updated: Oct 26, 2026

Use of Stopped-Flow Fluorescence and Labeled Nucleotides to Analyze the ATP Turnover Cycle of Kinesins
Published on: October 17, 2014
The structural and mechanochemical cycle of kinesin
1Max Planck Unit for Structural Molecular Biology, Hamburg, Germany. mand@mpasmb.desy.de
Abstract:
Kinesin is a microtubule-based motor protein that pulls vesicles or organelles towards the plus end of microtubules. Structural changes in the protein that drive motility are coupled to ATP binding and hydrolysis. Here, we attempt to integrate recent structural and kinetic results into a picture of the mechanochemical cycle of kinesin.
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