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Related Concept Videos

Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...

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From Fast Fluorescence Imaging to Molecular Diffusion Law on Live Cell Membranes in a Commercial Microscope
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Fast Relaxation Imaging in living cells.

Apratim Dhar1, Martin Gruebele

  • 1University of Illinois, Urbana, Illinois, USA.

Current Protocols in Protein Science
|August 16, 2011
PubMed
Summary

Fast Relaxation Imaging (FReI) enables observing protein folding dynamics within living cells. This method allows direct comparison of in-cell and in vitro biomolecular processes with millisecond resolution.

Area of Science:

  • Biophysics
  • Cell Biology
  • Molecular Dynamics

Background:

  • Protein folding is crucial for cellular function.
  • Understanding in-cell protein dynamics is challenging.
  • Existing methods often lack cellular context or sufficient temporal resolution.

Purpose of the Study:

  • To describe a protocol for Fast Relaxation Imaging (FReI) applied to protein folding in living cells.
  • To detail the necessary modifications for fluorescence microscopy.
  • To enable direct comparison of in-cell and in vitro biomolecular processes.

Main Methods:

  • Modifications to a fluorescence microscope: diode laser temperature jump, switchable LED source, two-color CCD camera.
  • Protein labeling techniques for cellular imaging.

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  • Cell preparation for high-resolution kinetic imaging.
  • Acquisition of millisecond time-resolved movies of protein dynamics.

    • Main Results:

    • The protocol details the setup for FReI in living cells.
    • It outlines methods for protein labeling and cell preparation.
    • The technique achieves millisecond time resolution for in-cell kinetic studies.

    Conclusions:

    • FReI provides a powerful method for studying protein folding and other biomolecular processes in their native cellular environment.
    • Comparative in vitro and in-cell measurements can be performed on the same setup.
    • This facilitates understanding the differences between cellular and solution-phase biomolecular dynamics.