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What Molecular Dynamics Simulations Can Tell Us About Mechanical Properties of Kinesin and Its Interaction With Tubulin

[+] Author Affiliations
Iuliana Aprodu, Alfonso Gautieri, Alberto Redaelli, Monica Soncini

Politecnico di Milano, Milano, Italy

Franco M. Montevecchi

Politecnico di Torino, Turin, Italy

Paper No. SBC2007-176316, pp. 781-782; 2 pages
  • ASME 2007 Summer Bioengineering Conference
  • ASME 2007 Summer Bioengineering Conference
  • Keystone, Colorado, USA, June 20–24, 2007
  • Conference Sponsors: Bioengineering Division
  • ISBN: 0-7918-4798-5
  • Copyright © 2007 by ASME


Kinesin is a processive molecular motor found in various cells including neurons, that transports membrane-bound vesicles and organelles along the microtubule. Kinesin typically consists of three distinct domains: two large globular heads that attach to the microtubule, a central coiled region, and a light-chain that attaches to the cellular cargo. The metabolic energy that drives kinesins is provided in the form of ATP. The energy released by ATP hydrolysis is converted into direct movement after kinesin binds strongly to the microtubule. Two mechanisms were proposed to explain the movement of kinesin along microtubules: the “hand over hand” model in which the two heads alternate in the role of leading and the “inchworm” model in which one head always leads.

Copyright © 2007 by ASME



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