A structural perspective on the dynamics of kinesin motors

Abstract

Despite significant fluctuation under thermal noise, biological machines in cells perform their tasks with exquisite precision. Using molecular simulation of a coarse-grained model and theoretical arguments we envisaged how kinesin, a prototype of biological machines, generates force and regulates its dynamics to sustain persistent motor action. A structure based model, which can be versatile in adapting its structure to external stresses while maintaining its native fold, was employed to account for several features of kinesin dynamics along the biochemical cycle. This analysis complements our current understandings of kinesin dynamics and connections to experiments. We propose a thermodynamic cycle for kinesin that emphasizes the mechanical and regulatory role of the neck-linker and clarify issues related the motor directionality, and the difference between the external stalling force and the internal tension responsible for the head-head coordination. The comparison between the thermodynamic cycle of kinesin and macroscopic heat engines highlights the importance of structural change as the source of work production in biomolecular machines.

35 pages, 8 figures, 1 Table

References in corpus (4)

• Capturing the essence of folding and functions of biomolecules using Coarse-Grained Models
• Dynamics of allosteric transitions in GroEL
• Internal strain regulates the nucleotide binding site of the kinesin leading head
• Mechanical control of the directional stepping dynamics of the kinesin motor

Cited by in corpus (8)

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• Generalized Iterative Annealing Model for the action of RNA chaperones
• Analysis of kinesin mechanochemistry via simulated annealing
• Symmetry, Rigidity, and Allosteric Signaling: From Monomeric Proteins to Molecular Machines
• How kinesin waits for ATP affects the nucleotide and load dependence of the stepping kinetics