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

14.9K
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...
14.9K
Ligand Binding Sites02:40

Ligand Binding Sites

15.4K
Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
15.4K
Protein and Protein Structure02:15

Protein and Protein Structure

90.0K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
90.0K
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

3.7K
Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
3.7K

You might also read

Related Articles

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

Sort by
Same author

Gestational diabetes alters subgingival pathobiont composition.

Acta odontologica Scandinavica·2026
Same author

Fabrication of UF-white cheese: Obtaining a different proteolysis rate, texture, and flavor via using combinations of mesophilic starter culture and <i>Lactobacillus helveticus</i>.

Food science & nutrition·2024
Same author

Rheology and Gelation of Hyaluronic Acid/Chitosan Coacervates.

Biomolecules·2022
Same author

Solubilization of concentrated protein dispersion: Effect of hydrogen peroxide (H<sub>2</sub>O<sub>2</sub>) and sodium hexametaphosphate (SHMP).

Food chemistry·2022
Same author

Copper-binding anticancer peptides from the piscidin family: an expanded mechanism that encompasses physical and chemical bilayer disruption.

Scientific reports·2021
Same author

High-Pressure Carbon Dioxide Use to Control Dried Apricot Pests, <i>Tribolium castaneum</i> and <i>Rhyzopertha dominica</i>, and Assessing the Qualitative Traits of Dried Pieces of Treated Apricot.

Foods (Basel, Switzerland)·2021

Related Experiment Video

Updated: Feb 25, 2026

Determination of Zeta Potential via Nanoparticle Translocation Velocities through a Tunable Nanopore: Using DNA-modified Particles as an Example
08:42

Determination of Zeta Potential via Nanoparticle Translocation Velocities through a Tunable Nanopore: Using DNA-modified Particles as an Example

Published on: October 26, 2016

12.8K

Polysaccharide zeta-potentials and protein-affinity.

Fatih Comert1, Fatemeh Azarikia, Paul L Dubin

  • 1Department of Chemistry, University of Massachusetts Amherst, 710 North Pleasant Street, Amherst, Massachusetts 01003, USA. dubin@chem.umass.edu.

Physical Chemistry Chemical Physics : PCCP
|August 10, 2017
PubMed
Summary
This summary is machine-generated.

Zeta-potential measurements do not always predict polysaccharide-protein binding affinity. Different polysaccharide structures, like hyaluronic acid and tragacanthin, can bind differently to proteins even with similar zeta-potentials.

More Related Videos

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
08:53

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Published on: October 2, 2017

31.7K
Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

2.6K

Related Experiment Videos

Last Updated: Feb 25, 2026

Determination of Zeta Potential via Nanoparticle Translocation Velocities through a Tunable Nanopore: Using DNA-modified Particles as an Example
08:42

Determination of Zeta Potential via Nanoparticle Translocation Velocities through a Tunable Nanopore: Using DNA-modified Particles as an Example

Published on: October 26, 2016

12.8K
Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
08:53

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Published on: October 2, 2017

31.7K
Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

2.6K

Area of Science:

  • Biophysical Chemistry
  • Food Science
  • Materials Science

Background:

  • Zeta-potential is commonly used to assess electrostatic interactions in polysaccharide-protein complexation.
  • Understanding these interactions is crucial for applications in food, pharmaceuticals, and biomaterials.

Purpose of the Study:

  • To investigate if identical zeta-potentials of two anionic polysaccharides (hyaluronic acid and tragacanthin) correlate with equal binding affinity to beta-lactoglobulin (BLG).
  • To elucidate the influence of polysaccharide structure on electrostatic interactions with proteins.

Main Methods:

  • Precise turbidimetric titrations to determine critical pH values for complex formation between polysaccharides and BLG.
  • Measurement of polysaccharide zeta-potentials at various ionic strengths and critical pH values.
  • Comparative analysis of binding affinities based on phase boundaries and fixed zeta-potential.

Main Results:

  • Phase boundary analysis indicated stronger binding of hyaluronic acid to BLG compared to tragacanthin.
  • However, comparisons at identical zeta-potentials suggested stronger binding for tragacanthin.
  • This discrepancy arises from the influence of tragacanthin's bulky side chains on its friction coefficient and mobility, affecting zeta-potential measurements independently of direct BLG interaction.

Conclusions:

  • Zeta-potential alone is an insufficient predictor of polysaccharide-protein binding affinity when polysaccharide structures differ significantly.
  • The shear plane location relative to the bound protein is critical for zeta-potential's relevance in electrostatic interactions.
  • Polysaccharide structure, beyond surface charge, plays a vital role in complexation dynamics.