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Single-Molecule Spectroscopy of Motor Proteins

Nucleic Acids Structure and Mapping

  1. Bram Prevo,
  2. Seyda Acar,
  3. Dennis L.H. Kruijssen,
  4. Erwin J.G. Peterman

Published Online: 10 JAN 2014

DOI: 10.1002/9780470027318.a9267

Encyclopedia of Analytical Chemistry

Encyclopedia of Analytical Chemistry

How to Cite

Prevo, B., Acar, S., Kruijssen, D. L. and Peterman, E. J. 2014. Single-Molecule Spectroscopy of Motor Proteins. Encyclopedia of Analytical Chemistry. 1–25.

Author Information

  1. VU University Amsterdam, Amsterdam, The Netherlands

Publication History

  1. Published Online: 10 JAN 2014

Abstract

Single-molecule fluorescence spectroscopy has become a crucial tool to study the behavior of biomolecules and their roles in complex biological processes. Single-molecule methods have in particular contributed to our understanding of the mechanism of force generation and motility of motor proteins. Motor proteins are enzymes that convert the chemical free energy obtained from the hydrolysis of adenosine triphosphate (ATP) into mechanical work in order to drive processes such as muscle contraction and intracellular transport. Here, we review how single-molecule fluorescence spectroscopy can be applied to motor proteins of the kinesin, myosin, and dynein superfamilies and how such studies have advanced our knowledge of the molecular basis of motor protein action.