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

Tandem Mass Spectrometry01:21

Tandem Mass Spectrometry

3.0K
Tandem mass spectrometry is a technique that uses multiple mass analyzers in series to obtain a higher selectivity and reduce chemical noise during analyte detection. Instruments with multiple analyzers separated by an interaction cell enable secondary fragmentation and selected study of the fragment ions.Secondary fragmentations occur in the interaction cell and can be induced by various factors. Fragmentation induced by collision with inert gases, such as N2, Ar, He, etc., is called...
3.0K

You might also read

Related Articles

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

Sort by
Same author

Cooperativity, dynamics, and the free-energy surfaces of charge-patterned IDPs.

bioRxiv : the preprint server for biology·2026
Same author

Dissecting mechanisms of ligand binding and conformational changes in the glutamine-binding protein.

eLife·2026
Same author

Time-Resolved Single-Molecule FRET Reveals Length-Dependent Nucleosome Decompaction by Poly(ADP-ribose).

bioRxiv : the preprint server for biology·2026
Same author

Dynamical Buffering of Reconfiguration Dynamics in Intrinsically Disordered Proteins.

JACS Au·2026
Same author

Toward a unified framework for determining conformational ensembles of disordered proteins.

Nature methods·2026
Same author

Mapping Charge Interactions in Intrinsically Disordered Proteins.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2025

Related Experiment Video

Updated: May 5, 2026

Fluorescence detection methods for microfluidic droplet platforms
14:16

Fluorescence detection methods for microfluidic droplet platforms

Published on: December 10, 2011

24.8K

Rapid Microfluidic Double-Jump Mixing Device for Single-Molecule Spectroscopy.

Fabian Dingfelder1, Bengt Wunderlich1, Stephan Benke1

  • 1Department of Biochemistry, University of Zurich , Winterthurerstrasse 190, 8057 Zurich, Switzerland.

Journal of the American Chemical Society
|April 11, 2017
PubMed
Summary

A new microfluidic device allows scientists to study fast biomolecular reactions and transient states. This method enhances single-molecule spectroscopy for exploring complex protein dynamics and interactions.

More Related Videos

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

16.1K
Multicolor Fluorescence Detection for Droplet Microfluidics Using Optical Fibers
10:21

Multicolor Fluorescence Detection for Droplet Microfluidics Using Optical Fibers

Published on: May 5, 2016

10.6K

Related Experiment Videos

Last Updated: May 5, 2026

Fluorescence detection methods for microfluidic droplet platforms
14:16

Fluorescence detection methods for microfluidic droplet platforms

Published on: December 10, 2011

24.8K
Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

16.1K
Multicolor Fluorescence Detection for Droplet Microfluidics Using Optical Fibers
10:21

Multicolor Fluorescence Detection for Droplet Microfluidics Using Optical Fibers

Published on: May 5, 2016

10.6K

Area of Science:

  • Biophysics
  • Chemical Kinetics
  • Molecular Biology

Background:

  • Investigating rapid biomolecular kinetics is crucial for understanding complex biological processes.
  • Existing single-molecule approaches face limitations in probing transiently populated intermediates and nonequilibrium dynamics.
  • Confocal single-molecule spectroscopy is a powerful tool but requires enhanced mixing capabilities for faster kinetics.

Purpose of the Study:

  • To introduce a novel microfluidic double-jump mixing device for high-resolution kinetic studies.
  • To enable the investigation of nonequilibrium dynamics and transient states in biomolecular reactions.
  • To demonstrate the device's capability in studying complex protein folding and conformational changes.

Main Methods:

  • Development and implementation of a microfluidic double-jump mixing device.
  • Utilizing confocal single-molecule spectroscopy for real-time observation.
  • Applying the device to study coupled folding-binding reactions of intrinsically disordered proteins.
  • Analyzing conformational changes in a large cytolytic pore-forming toxin.

Main Results:

  • The microfluidic device successfully probes biomolecular kinetics on time scales from milliseconds to minutes.
  • Transiently populated intermediates, previously inaccessible, were observed.
  • The coupled folding and binding of two intrinsically disordered proteins were investigated.
  • Conformational dynamics of a cytolytic toxin were characterized.

Conclusions:

  • The microfluidic double-jump mixing device is a reliable and powerful tool for studying rapid biomolecular kinetics.
  • This technology expands the accessible time scales and dynamic regimes for single-molecule investigations.
  • The method provides new insights into the mechanisms of protein folding, binding, and conformational transitions.