Use of single molecule fluorescence polarization microscopy to study protein conformation and dynamics of kinesin–microtubule complexes

Research output: Chapter in Book/Report/Conference proceedingChapter

1 Citation (Scopus)

Abstract

Single molecule fluorescence polarization microscopy (smFPM) is a technique that enables to monitor changes in the orientation of a single labeled protein domain. Here we describe a smFPM microscope set-up and protocols to investigate conformational changes associated with the movement of motor proteins along cytoskeletal tracks.

Original languageEnglish (US)
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Pages199-216
Number of pages18
Volume1665
DOIs
StatePublished - 2018

Publication series

NameMethods in Molecular Biology
Volume1665
ISSN (Print)1064-3745

Fingerprint

Polarization Microscopy
Protein Conformation
Fluorescence Polarization
Fluorescence Microscopy
Cytoskeletal Proteins
Single Molecule Imaging
Protein Domains

Keywords

  • BSR
  • Dichroism
  • Fluorescence polarization
  • Kinesin
  • Microtubule
  • Molecular motor
  • Single molecule

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

Cite this

Use of single molecule fluorescence polarization microscopy to study protein conformation and dynamics of kinesin–microtubule complexes. / Benoit, Matthieu P.M.H.; Sosa, Hernando.

Methods in Molecular Biology. Vol. 1665 Humana Press Inc., 2018. p. 199-216 (Methods in Molecular Biology; Vol. 1665).

Research output: Chapter in Book/Report/Conference proceedingChapter

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