Single-molecule fluorescence spectroscopy and microscopy of biomolecular motors

Erwin J.G. Peterman, Hernando Sosa, W. E. Moerner

Research output: Contribution to journalArticle

118 Scopus citations

Abstract

The methods of single-molecule fluorescence spectroscopy and microscopy have been recently utilized to explore the mechanism of action of several members of the kinesin and myosin biomolecular motor protein families. Whereas ensemble averaging is removed in single-molecule studies, heterogeneity in the behavior of individual motors can be directly observed, without synchronization. Observation of translocation by individual copies of motor proteins allows analysis of step size, rate, pausing, and other statistical properties of the process. Polarization microscopy as a function of nucleotide state has been particularly useful in revealing new and highly rotationally mobile forms of particular motors. These experiments complement X-ray and biochemical studies and provide a detailed view into the local dynamical behavior of motor proteins.

Original languageEnglish (US)
Pages (from-to)79-96
Number of pages18
JournalAnnual Review of Physical Chemistry
Volume55
DOIs
StatePublished - Aug 9 2004

Keywords

  • Kinesin
  • Molecular motor proteins
  • Myosin
  • Single biomolecule detection

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry

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