Structure and dynamics of the kinesin-microtubule interaction revealed by fluorescence polarization microscopy

Hernando J. Sosa, Ana B. Asenjo, Erwin J G Peterman

Research output: Book/ReportBook

6 Citations (Scopus)

Abstract

Fluorescence polarization microscopy (FPM) is the analysis of the polarization of light in a fluorescent microscope in order to determine the angular orientation and rotational mobility of fluorescent molecules. Key advantages of FPM, relative to other structural analysis techniques, are that it allows the detection of conformational changes of fluorescently labeled macromolecules in real time in physiological conditions and at the single-molecule level. In this chapter we describe in detail the FPM experimental set-up and analysis methods we have used to investigate structural intermediates of the motor protein kinesin-1 associated with its walking mechanism along microtubules. We also briefly describe additional FPM methods that have been used to investigate other macromolecular complexes.

Original languageEnglish (US)
PublisherUnknown Publisher
Number of pages15
Volume95
EditionC
DOIs
StatePublished - 2010

Publication series

NameMethods in Cell Biology
No.C
Volume95
ISSN (Print)0091679X

Fingerprint

Polarization Microscopy
Kinesin
Fluorescence Polarization
Fluorescence Microscopy
Microtubules
Macromolecular Substances
Walking
Light
Proteins

ASJC Scopus subject areas

  • Cell Biology

Cite this

Structure and dynamics of the kinesin-microtubule interaction revealed by fluorescence polarization microscopy. / Sosa, Hernando J.; Asenjo, Ana B.; Peterman, Erwin J G.

C ed. Unknown Publisher, 2010. 15 p. (Methods in Cell Biology; Vol. 95, No. C).

Research output: Book/ReportBook

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