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Use of Single Molecule Fluorescence Polarization Microscopy to Study Protein Conformation and Dynamics of

Matthieu P M H Benoit1, Hernando Sosa2

  • 1Department of Physiology and Biophysics, Albert Einstein College of Medicine, Jack and Pearl Resnick Campus, 1300 Morris Park Avenue, Bronx, NY, 10461, USA.

Methods in Molecular Biology (Clifton, N.J.)
|September 24, 2017
PubMed

Insights

Single molecule fluorescence polarization microscopy (smFPM) monitors protein orientation changes. This study details an smFPM setup for observing motor protein conformational changes during movement along cytoskeletal tracks.

Area of Science:

  • Biophysics
  • Cell Biology
  • Microscopy

Background:

  • Single molecule fluorescence polarization microscopy (smFPM) is a powerful technique.
  • Monitoring protein domain orientation changes is crucial for understanding molecular mechanisms.

Purpose of the Study:

  • To describe a novel smFPM microscope setup.
  • To provide protocols for investigating motor protein conformational dynamics.

Main Methods:

  • Development and implementation of a specialized smFPM microscope.
  • Application of smFPM to study motor protein movement along cytoskeletal tracks.

Main Results:

  • The described smFPM setup allows for precise monitoring of single labeled protein domain orientations.
  • Conformational changes associated with motor protein activity were successfully investigated.

Conclusions:

  • The presented smFPM approach offers a robust method for studying protein dynamics.
  • This technique facilitates deeper understanding of motor protein function in cellular processes.
Keywords:
BSRDichroismFluorescence polarizationKinesinMicrotubuleMolecular motorSingle molecule

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