Noise-induced acceleration of single molecule kinesin-1

TL;DR

This study demonstrates that external noise can accelerate kinesin-1 movement, especially under hindering loads, and aligns with a kinetic model suggesting a universal noise-utilization mechanism in cellular enzymes.

Contribution

It provides experimental evidence of noise-induced acceleration in kinesin-1 and links it to a universal kinetic theory applicable to intracellular enzymes.

Findings

Kinesin accelerates under noisy forces, especially with hindering loads.

The behavior matches a simple two-state reaction model.

Active cellular fluctuations may be exploited to enhance enzyme function.

Abstract

The movement of single kinesin molecules was observed while applying noisy external forces that mimic intracellular active fluctuations. We found kinesin accelerates under noise, especially when a large hindering load is added. The behavior quantitatively conformed to a theoretical model that describes the kinesin movement with simple two-state reactions. The universality of the kinetic theory suggests that intracellular enzymes share a similar noise-induced acceleration mechanism, i.e. active fluctuations in cells are not just noise but are utilized to promote various physiological processes.