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

8% capsaicin patches for HIV-induced polyneuropathy: a systematic review and meta-analysis.

Pain management·2026

Same author

Refractory Chronic Neuropathic Pain Successfully Treated With Scrambler Therapy.

The primary care companion for CNS disorders·2026

Same author

Intrathecal baclofen pump failure due to pain-induced autonomic dysreflexia.

BMJ case reports·2026

Same author

Evaluation of the Gigstride wearable device for pain reduction and functional outcomes in patients with lower extremity mobility deficits: a single-arm pilot feasibility study.

Pain management·2026

Same author

Inferior Outcomes of p230-CML with Imatinib: a Report of 2 Cases of p210/p230 Co-Expressed CML Showing Rapid Progression To Leukaemia Cutis along with the Systematic Review.

Indian journal of hematology & blood transfusion : an official journal of Indian Society of Hematology and Blood Transfusion·2026

Same author

Polyamine homeostasis in Caenorhabditis elegans relies primarily on transport.

Cell reports·2026

Same journal

Daily briefing: 'Cyborg' cockroaches breathe underwater with printed suit.

Nature·2026

Same journal

China boosts prestigious grants for young scientists - will it ease competition?

Nature·2026

Same journal

Incoming US science academy chief vows to 'double down' on research.

Nature·2026

Same journal

Author Correction: Synthesis of enantioenriched atropisomers by biocatalytic deracemization.

Nature·2026

Same journal

Electrodeposited self-assembled molecules for perovskite photovoltaics.

Nature·2026

Same journal

Neutrino's nursery found: the 'Shadow Blaster'.

Nature·2026

See all related articles

Search research articles

Related Experiment Video

Updated: May 5, 2026

Combining Single-molecule Manipulation and Imaging for the Study of Protein-DNA Interactions

Combining Single-molecule Manipulation and Imaging for the Study of Protein-DNA Interactions

Published on: August 27, 2014

Probing cellular protein complexes using single-molecule pull-down.

Ankur Jain¹, Ruijie Liu, Biswarathan Ramani

¹Center for Biophysics and Computational Biology and Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.

|May 27, 2011

Summary

This summary is machine-generated.

This study introduces the single-molecule pull-down (SiMPull) assay to visualize individual protein complexes within cells. This method reveals the composition and functionality of protein assemblies in various biological pathways.

More Related Videos

Identification of Small Molecule-binding Proteins in a Native Cellular Environment by Live-cell Photoaffinity Labeling

Identification of Small Molecule-binding Proteins in a Native Cellular Environment by Live-cell Photoaffinity Labeling

Published on: September 20, 2016

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

Related Experiment Videos

Last Updated: May 5, 2026

Combining Single-molecule Manipulation and Imaging for the Study of Protein-DNA Interactions

Combining Single-molecule Manipulation and Imaging for the Study of Protein-DNA Interactions

Published on: August 27, 2014

Identification of Small Molecule-binding Proteins in a Native Cellular Environment by Live-cell Photoaffinity Labeling

Identification of Small Molecule-binding Proteins in a Native Cellular Environment by Live-cell Photoaffinity Labeling

Published on: September 20, 2016

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

Area of Science:

Biochemistry
Molecular Biology
Cell Biology

Background:

Proteins execute cellular functions through macromolecular complexes.
Proteins often participate in multiple complexes, leading to diverse functions.
Existing methods struggle to capture the dynamic permutations of protein interactions in vivo.

Purpose of the Study:

To develop a novel assay for visualizing and analyzing individual cellular protein complexes.
To overcome limitations of ensemble approaches in studying protein interaction permutations.
To enable direct visualization of protein complex composition and stoichiometry.

Main Methods:

Development of the single-molecule pull-down (SiMPull) assay.
Integration of conventional pull-down techniques with single-molecule fluorescence microscopy.
Application to various signaling proteins and endogenous complexes from animal tissues.

Main Results:

SiMPull enables direct visualization of individual protein complexes.
The assay accurately determines the number and types of proteins within a complex, demonstrated with protein kinase A.
Demonstrated broad applicability across cellular compartments and endogenous extracts.
Pulled-down proteins remain functional for subsequent single-molecule biochemical studies.

Conclusions:

SiMPull is a sensitive, rapid, and robust platform for analyzing protein assemblies.
Provides unprecedented insight into the composition and dynamics of protein complexes.
Facilitates deeper understanding of protein complex roles in biological pathways.