Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1996 Jun 25;93(13):6775–6779. doi: 10.1073/pnas.93.13.6775

The kinesin walk: a dynamic model with elastically coupled heads.

I Derényi 1, T Vicsek 1
PMCID: PMC39103  PMID: 8692894

Abstract

Recently individual two-headed kinesin molecules have been studied in in vitro motility assays revealing a number of their peculiar transport properties. In this paper we propose a simple and robust model for the kinesin stepping process with elastically coupled Brownian heads that show all of these properties. The analytic and numerical treatment of our model results in a very good fit to the experimental data and practically has no free parameters. Changing the values of the parameters in the restricted range allowed by the related experimental estimates has almost no effect on the shape of the curves and results mainly in a variation of the zero load velocity that can be directly fitted to the measured data. In addition, the model is consistent with the measured pathway of the kinesin ATPase.

Full text

PDF
6778

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Astumian RD, Bier M. Fluctuation driven ratchets: Molecular motors. Phys Rev Lett. 1994 Mar 14;72(11):1766–1769. doi: 10.1103/PhysRevLett.72.1766. [DOI] [PubMed] [Google Scholar]
  2. Doering CR, Horsthemke W, Riordan J. Nonequilibrium fluctuation-induced transport. Phys Rev Lett. 1994 May 9;72(19):2984–2987. doi: 10.1103/PhysRevLett.72.2984. [DOI] [PubMed] [Google Scholar]
  3. Fenn W. O. The relation between the work performed and the energy liberated in muscular contraction. J Physiol. 1924 May 23;58(6):373–395. doi: 10.1113/jphysiol.1924.sp002141. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Gilbert S. P., Webb M. R., Brune M., Johnson K. A. Pathway of processive ATP hydrolysis by kinesin. Nature. 1995 Feb 23;373(6516):671–676. doi: 10.1038/373671a0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Hirose K., Lockhart A., Cross R. A., Amos L. A. Nucleotide-dependent angular change in kinesin motor domain bound to tubulin. Nature. 1995 Jul 20;376(6537):277–279. doi: 10.1038/376277a0. [DOI] [PubMed] [Google Scholar]
  6. Hoenger A., Sablin E. P., Vale R. D., Fletterick R. J., Milligan R. A. Three-dimensional structure of a tubulin-motor-protein complex. Nature. 1995 Jul 20;376(6537):271–274. doi: 10.1038/376271a0. [DOI] [PubMed] [Google Scholar]
  7. Hunt A. J., Gittes F., Howard J. The force exerted by a single kinesin molecule against a viscous load. Biophys J. 1994 Aug;67(2):766–781. doi: 10.1016/S0006-3495(94)80537-5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Kikkawa M., Ishikawa T., Wakabayashi T., Hirokawa N. Three-dimensional structure of the kinesin head-microtubule complex. Nature. 1995 Jul 20;376(6537):274–277. doi: 10.1038/376274a0. [DOI] [PubMed] [Google Scholar]
  9. Magnasco MO. Forced thermal ratchets. Phys Rev Lett. 1993 Sep 6;71(10):1477–1481. doi: 10.1103/PhysRevLett.71.1477. [DOI] [PubMed] [Google Scholar]
  10. Millonas MM. Self-consistent microscopic theory of fluctuation-induced transport. Phys Rev Lett. 1995 Jan 2;74(1):10–13. doi: 10.1103/PhysRevLett.74.10. [DOI] [PubMed] [Google Scholar]
  11. Prost J, Chauwin JF, Peliti L, Ajdari A. Asymmetric pumping of particles. Phys Rev Lett. 1994 Apr 18;72(16):2652–2655. doi: 10.1103/PhysRevLett.72.2652. [DOI] [PubMed] [Google Scholar]
  12. Ray S., Meyhöfer E., Milligan R. A., Howard J. Kinesin follows the microtubule's protofilament axis. J Cell Biol. 1993 Jun;121(5):1083–1093. doi: 10.1083/jcb.121.5.1083. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Rayment I., Holden H. M., Whittaker M., Yohn C. B., Lorenz M., Holmes K. C., Milligan R. A. Structure of the actin-myosin complex and its implications for muscle contraction. Science. 1993 Jul 2;261(5117):58–65. doi: 10.1126/science.8316858. [DOI] [PubMed] [Google Scholar]
  14. Song Y. H., Mandelkow E. Recombinant kinesin motor domain binds to beta-tubulin and decorates microtubules with a B surface lattice. Proc Natl Acad Sci U S A. 1993 Mar 1;90(5):1671–1675. doi: 10.1073/pnas.90.5.1671. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Svoboda K., Block S. M. Force and velocity measured for single kinesin molecules. Cell. 1994 Jun 3;77(5):773–784. doi: 10.1016/0092-8674(94)90060-4. [DOI] [PubMed] [Google Scholar]
  16. Svoboda K., Mitra P. P., Block S. M. Fluctuation analysis of motor protein movement and single enzyme kinetics. Proc Natl Acad Sci U S A. 1994 Dec 6;91(25):11782–11786. doi: 10.1073/pnas.91.25.11782. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Svoboda K., Schmidt C. F., Schnapp B. J., Block S. M. Direct observation of kinesin stepping by optical trapping interferometry. Nature. 1993 Oct 21;365(6448):721–727. doi: 10.1038/365721a0. [DOI] [PubMed] [Google Scholar]
  18. Vale R. D., Reese T. S., Sheetz M. P. Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility. Cell. 1985 Aug;42(1):39–50. doi: 10.1016/s0092-8674(85)80099-4. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. de Paula J. C., Robblee J. H., Pasternack R. F. Aggregation of chlorophyll a probed by resonance light scattering spectroscopy. Biophys J. 1995 Jan;68(1):335–341. doi: 10.1016/S0006-3495(95)80192-X. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES