Single-molecule fluorescence spectroscopy and microscopy of biomolecular motors

E.J.G. Peterman, H. Sosa, W. E. Moerner

Research output: Contribution to JournalArticleAcademicpeer-review

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
Pages (from-to)79-96
JournalAnnual Review of Physical Chemistry
Volume55
DOIs
Publication statusPublished - 2004

Bibliographical note

Single-molecule fluorescence spectroscopy and microscopy of biomolecular motors

Fingerprint

Dive into the research topics of 'Single-molecule fluorescence spectroscopy and microscopy of biomolecular motors'. Together they form a unique fingerprint.

Cite this