How occasional backstepping can speed up a processive motor protein

TL;DR

This paper explores how occasional backsteps in kinesin motor proteins can enhance their overall speed by increasing entropy production, revealing an optimal backstep rate for maximum forward velocity.

Contribution

It introduces a model linking backstep frequency to entropy production and speed optimization in kinesin, a novel perspective on motor protein efficiency.

Findings

Backstepping correlates with increased entropy production.

An optimal backstep percentage maximizes net forward speed.

Measured backstep rates align with the predicted optimum.

Abstract

Fueled by the hydrolysis of ATP, the motor protein kinesin literally walks on two legs along the biopolymer microtubule. The number of accidental backsteps that kinesin takes appears to be much larger than what one would expect given the amount of free energy that ATP hydrolysis makes available. This is puzzling as more than a billion years of natural selection should have optimized the motor protein for its speed and efficiency. But more backstepping allows for the production of more entropy. Such entropy production will make free energy available. With this additional free energy, the catalytic cycle of the kinesin can be speeded up. We show how measured backstep percentages represent an optimum at which maximal net forward speed is achieved.