Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

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...
Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...

You might also read

Related Articles

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

Sort by
Same author

Numerical characterization of electrochemical transport in three-dimensional rhombic zero-depth pores.

Scientific reports·2026
Same author

Reconstruction of the radiological component of the exposome in the CONSTANCES cohort.

The Science of the total environment·2026
Same author

Fabrication of Sub-50 nm Three-Dimensional Rhombic Zero-Depth PDMS Nanopores with Enhanced Conductance via Silicon Micro-Blade Molding.

Micromachines·2025
Same author

A Radical Cascade with Double Intramolecular Hydrogen Atom Transfer for the Generation of Bisfunctionalized Cyclopentanes from Linear Alkynes.

Angewandte Chemie (International ed. in English)·2025
Same author

Kinematic Alterations with Changes in Putting Distance and Slope Incline in Recreational Golfers.

Bioengineering (Basel, Switzerland)·2025
Same author

Photochemical Synthesis of Lactones, Cyclopropanes and ATRA Products: Revealing the Role of Sodium Ascorbate.

Chemistry (Weinheim an der Bergstrasse, Germany)·2024
Same journal

Analyses of dextroamphetamine and its metabolites in human urine by capillary electrophoresis with diode array and capacitively coupled contactless conductivity detection (CE-DAD-C<sup>4</sup>D).

Analytical and bioanalytical chemistry·2026
Same journal

Whole-body mass spectrometry imaging reveals metabolome and lipid peroxidation heterogeneity in zebrafish xenografts of esophageal squamous cell carcinoma.

Analytical and bioanalytical chemistry·2026
Same journal

A robust and validated method for the determination of 21 urinary metabolites of 15 plasticizers, including phthalates, DEHTP, and DINCH, by online SPE and liquid chromatography-tandem mass spectrometry.

Analytical and bioanalytical chemistry·2026
Same journal

A label-free membrane-based biosensor array with AuNP-modified PDMS for sensitive and specific detection of alpha-fetoprotein.

Analytical and bioanalytical chemistry·2026
Same journal

Smartphone-integrated one-step colorimetric glucose detection at physiological pH enabled by a haloperoxidase mimic.

Analytical and bioanalytical chemistry·2026
Same journal

Chemiluminescence functionalized magnetic nanoparticles-based biosensor for sensitive detection of glucose, uric acid, and cholesterol.

Analytical and bioanalytical chemistry·2026
See all related articles

Related Experiment Video

Updated: Jun 27, 2026

Analysis of Protein Complex Formation at Micromolar Concentrations by Coupling Microfluidics with Mass Photometry
06:39

Analysis of Protein Complex Formation at Micromolar Concentrations by Coupling Microfluidics with Mass Photometry

Published on: January 26, 2024

Detecting proteins complex formation using steady-state diffusion in a nanochannel.

Nicolas F Y Durand1, Elli Saveriades, Philippe Renaud

  • 1Microsystems Laboratory, STI-LMIS, EPFL, 1015, Lausanne, Switzerland. nicolas.durand@epfl.ch

Analytical and Bioanalytical Chemistry
|December 17, 2008
PubMed
Summary
This summary is machine-generated.

This study introduces nanofluidic channels as a novel biosensor for detecting rapid protein complex formation. The research demonstrates a simple technique to measure protein binding affinity by observing diffusion profiles in nanochannels.

More Related Videos

Monitoring Protein Adsorption with Solid-state Nanopores
08:51

Monitoring Protein Adsorption with Solid-state Nanopores

Published on: December 2, 2011

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

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: Jun 27, 2026

Analysis of Protein Complex Formation at Micromolar Concentrations by Coupling Microfluidics with Mass Photometry
06:39

Analysis of Protein Complex Formation at Micromolar Concentrations by Coupling Microfluidics with Mass Photometry

Published on: January 26, 2024

Monitoring Protein Adsorption with Solid-state Nanopores
08:51

Monitoring Protein Adsorption with Solid-state Nanopores

Published on: December 2, 2011

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

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:

  • Biophysics
  • Nanotechnology
  • Biochemistry

Background:

  • Nanofluidic channels offer unique properties for biomolecule analysis.
  • Confined spaces in nanofluidics alter effective diffusion rates.
  • Measuring rapid protein complex formation is crucial for biological studies.

Purpose of the Study:

  • To investigate nanofluidic channels as biosensors for protein complex formation.
  • To develop a theoretical model for protein diffusion in nanoslits.
  • To experimentally validate the detection of protein binding affinity.

Main Methods:

  • Theoretical modeling of protein concentration profiles in nanoslits.
  • Experimental measurement of fluorescent diffusion profiles.
  • Utilizing specific protein interactions (streptavidin-biotinylated dextran) for validation.

Main Results:

  • A theoretical model predicts wider diffusion profiles for protein complexes compared to single proteins.
  • Experimental data confirm increased fluorescent diffusion upon specific protein binding.
  • The technique successfully measured the affinity between streptavidin and biotinylated dextran.

Conclusions:

  • Nanofluidic channels provide a viable platform for biosensing rapid protein complex formation.
  • The observed changes in diffusion profiles can be directly correlated with protein binding affinity.
  • This method offers a direct and simplified approach for affinity measurements.