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Protein Dynamics in Living Cells

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...

Super-resolution Fluorescence Microscopy

Super-resolution Fluorescence Microscopy

Super-resolution fluorescence microscopy (SRFM) provides a better resolution than conventional fluorescence microscopy by reducing the point spread function (PSF). PSF is the light intensity distribution from a point that causes it to appear blurred. Due to PSF, each fluorescing point appears bigger than its actual size, and it is the PSF interference of nearby fluorophores that causes the blurred image. Various approaches to achieving higher resolution through SRFM have recently been...

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Related Experiment Video

Updated: May 10, 2025

Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells

Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells

Published on: February 18, 2014

Resolving Conformational Plasticity in Mammalian Cells with High-Resolution Fluorescence Tools.

Hao Ruan^1,2, Edward A Lemke^1,3

¹BioCenter, Johannes Gutenberg University Mainz, Mainz, Germany;

Annual Review of Physical Chemistry

|April 21, 2025

Summary

This summary is machine-generated.

Investigating protein dynamics in cells reveals crucial insights into function and disease. New imaging technologies overcome limitations of in vitro studies for a more accurate understanding.

Keywords:

MINFLUX anisotropy fluorescence lifetime genetic code expansion in situ conformational plasticity single-molecule FRET

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Related Experiment Videos

Last Updated: May 10, 2025

Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells

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Published on: February 18, 2014

Micromanipulation Techniques Allowing Analysis of Morphogenetic Dynamics and Turnover of Cytoskeletal Regulators

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Published on: May 12, 2018

Visualizing the Conformational Dynamics of Membrane Receptors Using Single-Molecule FRET

Visualizing the Conformational Dynamics of Membrane Receptors Using Single-Molecule FRET

Published on: August 17, 2022

Area of Science:

Biophysics
Cellular Biology
Biochemistry

Background:

Understanding protein dynamics is vital for drug discovery and disease research.
Traditional methods using purified proteins do not reflect the complex cellular environment.
The intracellular milieu significantly influences protein structure and interactions.

Purpose of the Study:

To explore advanced fluorescence-based techniques for studying protein dynamics within mammalian cells.
To overcome the limitations of in vitro studies by investigating proteins in their native cellular context.
To provide a more accurate understanding of protein conformational plasticity and function.

Main Methods:

Utilizing fluorescence resonance energy transfer (FRET) to monitor protein proximity and conformational changes.
Employing fluorescence anisotropy to assess molecular motion and orientation.
Applying minimal photon flux imaging technologies for sensitive detection in live cells.

Main Results:

Demonstrated the capability of FRET and anisotropy to reveal intricate protein conformational dynamics in situ.
Showcased minimal photon flux imaging for high-resolution observation of dynamic structural changes.
Successfully captured protein behavior within the complex intracellular environment.

Conclusions:

Advanced fluorescence techniques offer a powerful approach to study protein dynamics in mammalian cells.
These methods provide a more comprehensive and accurate understanding compared to traditional in vitro approaches.
Directly investigating protein conformational plasticity in cells is key to advancing functional and disease mechanism studies.