Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

A Water-Soluble Diarylethene Base for Light-Controlled pH Modulation in Biological Systems.

Journal of the American Chemical Society·2026

Same author

Electric Double Layer Phenomena Near Surfaces Irreversibly Trigger Assembly of Tau Protein.

Journal of the American Chemical Society·2026

Same author

Surface Chemistry and Particle Morphology Govern the Multiscale Interactions and Properties of Silica-Polyelectrolyte-Stabilized Microcapsules.

Langmuir : the ACS journal of surfaces and colloids·2026

Same author

Electrochemically Driven Optical Dynamics of Reflectin Protein Films.

Advanced materials (Deerfield Beach, Fla.)·2025

Same author

Charge screening and hydrophobicity drive progressive assembly and liquid-liquid phase separation of reflectin protein.

The Journal of biological chemistry·2025

Same author

Protein Charge Neutralization Is the Proximate Driver Dynamically Tuning Reflectin Assembly.

International journal of molecular sciences·2024

Search research articles

Related Experiment Video

Updated: Jan 15, 2026

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Published on: July 17, 2019

FRET Dilution Assay for Analyzing Dynamic Exchange Between Protein Assemblies.

Reid Gordon¹, Daniel E Morse²

¹Department of Molecular, Cellular and Developmental Biology and the Institute for Collaborative Biotechnologies, University of California, Santa Barbara; reidwgordon@gmail.com.

Journal of Visualized Experiments : Jove

|October 6, 2025

Summary

This summary is machine-generated.

Researchers developed a new assay to study reflectin A1 protein assemblies, crucial for tunable iridescence. This method tracks protein movement in and out of assemblies, aiding biomaterial engineering.

More Related Videos

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale

Published on: March 14, 2019

Calibration-free In Vitro Quantification of Protein Homo-oligomerization Using Commercial Instrumentation and Free, Open Source Brightness Analysis Software

Calibration-free In Vitro Quantification of Protein Homo-oligomerization Using Commercial Instrumentation and Free, Open Source Brightness Analysis Software

Published on: July 17, 2018

Related Experiment Videos

Last Updated: Jan 15, 2026

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Published on: July 17, 2019

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale

Published on: March 14, 2019

Calibration-free In Vitro Quantification of Protein Homo-oligomerization Using Commercial Instrumentation and Free, Open Source Brightness Analysis Software

Calibration-free In Vitro Quantification of Protein Homo-oligomerization Using Commercial Instrumentation and Free, Open Source Brightness Analysis Software

Published on: July 17, 2018

Area of Science:

Biomaterials Science
Protein Biophysics
Structural Biology

Background:

Reflectin A1 protein drives tunable iridescence in cephalopods.
Its phase behavior is key for biomaterial engineering applications.
Protein net charge and salt concentration influence reflectin A1 assembly formation.

Purpose of the Study:

To characterize the dynamic exchange of proteins between reflectin A1 assemblies and the surrounding solution.
To develop a novel method for analyzing protein assembly dynamics.
To differentiate between dynamic and kinetically arrested protein assemblies.

Main Methods:

Utilized a novel fluorescence resonance energy transfer (FRET) dilution assay.
Combined FRET with dynamic light scattering (DLS) and protein concentration assays.
Investigated protein flux as a function of assembly age.

Main Results:

The novel FRET dilution assay successfully characterized the two-way flux of protein between reflectin A1 assemblies and a dilute phase.
The assay can distinguish between one-way and two-way protein flux during assembly formation.
Established a method to differentiate dynamic from arrested protein assemblies.

Conclusions:

The developed FRET dilution assay is a valuable tool for studying protein assembly dynamics.
This method can be adapted to investigate the biophysical origins of various protein assemblies.
Understanding reflectin A1 assembly dynamics is crucial for advancing biomaterial engineering.