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-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

You might also read

Related Articles

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

Sort by
Same author

Solvated Electron Generation from Coupled Plasmon Modes of Gold Nanoparticles Using Visible Light.

Nano letters·2026
Same author

Feature Selection and Hyperparameter Optimization for Machine Learned Classification of 3D Single-Particle Tracking.

Chemical & biomedical imaging·2026
Same author

D‑Blur: A Deep Learning Approach for Mapping Subdiffraction Diffusion with Motion-Blurred Images.

Chemical & biomedical imaging·2025
Same author

Plasmonic pathway to hybrid nanomaterials through energy transfer.

Science advances·2025
Same author

The Impact of Rare Adsorption Site Clustering on Peak Broadening in Chromatography.

Analytical chemistry·2025
Same author

Insights into the phase behavior at interfaces using vibrational sum frequency generation spectroscopy.

The Journal of chemical physics·2024

Related Experiment Video

Updated: Jun 19, 2026

Synthesis of an Intein-mediated Artificial Protein Hydrogel
15:06

Synthesis of an Intein-mediated Artificial Protein Hydrogel

Published on: January 27, 2014

12.5K

Imaging Switchable Protein Interactions with an Active Porous Polymer Support.

Chayan Dutta1, Logan D C Bishop1, Jorge Zepeda O2

  • 1Department of Chemistry, Rice University, Houston, Texas 77005, United States.

The Journal of Physical Chemistry. B
|May 23, 2020
PubMed
Summary

Stimuli-responsive hydrogels control protein transport via pH-induced structural changes. Physicochemical heterogeneity dictates protein confinement and desorption dynamics, optimizing biomaterial design.

More Related Videos

Preparation of Polypentafluorophenyl acrylate Functionalized SiO2 Beads for Protein Purification
08:51

Preparation of Polypentafluorophenyl acrylate Functionalized SiO2 Beads for Protein Purification

Published on: November 19, 2018

10.1K
Author Spotlight: Photo Switchable Protein Recruitment for Reversible Patterning in Artificial Cellular Systems
07:10

Author Spotlight: Photo Switchable Protein Recruitment for Reversible Patterning in Artificial Cellular Systems

Published on: February 23, 2024

1.5K

Related Experiment Videos

Last Updated: Jun 19, 2026

Synthesis of an Intein-mediated Artificial Protein Hydrogel
15:06

Synthesis of an Intein-mediated Artificial Protein Hydrogel

Published on: January 27, 2014

12.5K
Preparation of Polypentafluorophenyl acrylate Functionalized SiO2 Beads for Protein Purification
08:51

Preparation of Polypentafluorophenyl acrylate Functionalized SiO2 Beads for Protein Purification

Published on: November 19, 2018

10.1K
Author Spotlight: Photo Switchable Protein Recruitment for Reversible Patterning in Artificial Cellular Systems
07:10

Author Spotlight: Photo Switchable Protein Recruitment for Reversible Patterning in Artificial Cellular Systems

Published on: February 23, 2024

1.5K

Area of Science:

  • Biomaterials Science
  • Polymer Chemistry
  • Biophysics

Background:

  • Understanding protein transport at porous interfaces is crucial for biomaterial applications.
  • Stimuli-responsive hydrogels offer tunable control over protein capture and release.
  • Simultaneously monitoring protein transport and polymer structure presents an experimental challenge.

Purpose of the Study:

  • To investigate the relationship between hydrogel physicochemistry and protein transport dynamics.
  • To elucidate how pH-induced structural changes in hydrogels affect protein movement.
  • To establish a method for simultaneously observing protein transport and polymer structure.

Main Methods:

  • Utilized single-particle tracking (SPT) to monitor protein dynamics.
  • Employed fluorescence correlation spectroscopy Super-resolution Optical Fluctuation Imaging (fcsSOFI) to analyze interfacial polymer structure.
  • Investigated a pH-responsive hydrogel and model protein (lysozyme) system.

Main Results:

  • SPT revealed reversible switching of protein transport dynamics with pH changes.
  • fcsSOFI correlated hydrogel heterogeneity and pore structure with protein diffusion and adsorption/desorption.
  • Physicochemical heterogeneity was found to dictate protein confinement and desorption, especially in swollen hydrogels.

Conclusions:

  • Local hydrogel physicochemistry significantly influences protein transport mechanisms.
  • pH-responsive hydrogels provide tunable control over protein dynamics at interfaces.
  • The combined use of SPT and fcsSOFI enables simultaneous monitoring of protein transport and polymer structure changes.