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

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

8.6K
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
8.6K
Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

16.5K
For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
16.5K
Molecular Models02:00

Molecular Models

43.5K
Physical models representing molecular architectures of chemical compounds play essential roles in understanding chemistry. The use of molecular models makes it easier to visualize the structures and shapes of atoms and molecules.
43.5K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.9K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
2.9K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.1K
2.1K
Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

19.2K
19.2K

You might also read

Related Articles

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

Sort by
Same author

Unveiling the Intramolecular Thermodynamics of Multivalent Proteins: Exploratory Study on Engineered Protein Model.

Biomacromolecules·2026
Same author

Steric disruption of EGFR oligomerization overcomes therapy resistance in non-small cell lung cancer.

Science advances·2025
Same author

Supersaturation, Nucleation, and Phase Separation of Mesoscopic Systems.

Journal of the American Chemical Society·2025
Same author

Size-controlled assembly of phase separated protein condensates with interfacial protein cages.

Nature communications·2025
Same author

High order assembly of multiple protein cages with homogeneous sizes and shapes <i>via</i> limited cage surface engineering.

Chemical science·2023
Same author

Lipid coated protein condensates as stable protocells with selective uptake abilities for biomolecules.

Chemical science·2022

Related Experiment Video

Updated: Jan 16, 2026

Analyzing and Building Nucleic Acid Structures with 3DNA
16:24

Analyzing and Building Nucleic Acid Structures with 3DNA

Published on: April 26, 2013

21.2K

A Modular Protein-DNA Multimer Model to Explore How Valence and Monomer Affinity Shape Multivalent DNA Binding.

Hyoin Park1, Yongwon Jung1

  • 1Department of Chemistry, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 34141, Republic of Korea.

Analytical Chemistry
|October 1, 2025
PubMed
Summary

Multivalent interactions improve detection sensitivity but can reduce selectivity. This study found an optimal affinity range for DNA monomers that shifts to weaker affinities with increasing valency, enhancing detection performance.

More Related Videos

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
10:17

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

8.2K
Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells
06:48

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells

Published on: January 5, 2024

5.2K

Related Experiment Videos

Last Updated: Jan 16, 2026

Analyzing and Building Nucleic Acid Structures with 3DNA
16:24

Analyzing and Building Nucleic Acid Structures with 3DNA

Published on: April 26, 2013

21.2K
Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
10:17

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

8.2K
Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells
06:48

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells

Published on: January 5, 2024

5.2K

Area of Science:

  • Biochemistry and Molecular Biology
  • Biophysics
  • Materials Science

Background:

  • Multivalent interactions, driven by multiple weak binding events, enhance molecular recognition.
  • While multivalency boosts sensitivity, it can also increase nonspecific binding, impacting selectivity.
  • Understanding the interplay between valency, affinity, and detection is crucial for designing effective multivalent systems.

Purpose of the Study:

  • To investigate the impact of valency on DNA-protein interactions and detection performance.
  • To quantitatively analyze how multimerization affects sensitivity and selectivity across a range of monomeric affinities.
  • To establish quantitative trends for optimizing multivalent designs.

Main Methods:

  • Development of modular protein-DNA multimers with valencies from 1 to 4.
  • Quantitative analysis using surface plasmon resonance (SPR) and enzyme-linked immunosorbent assays (ELISA).
  • Systematic variation of monomeric DNA affinities (KD) from subnanomolar to millimolar.

Main Results:

  • Optimal DNA monomer affinity for detection shifted from nanomolar to micromolar with increased valency.
  • Monomers with KD ≥ ~50 μM showed limited signal enhancement even at tetrameric valency, indicating an affinity threshold.
  • A narrow affinity window for maximal selectivity was identified, shifting towards weaker affinities as valency increased.

Conclusions:

  • Increasing valency shifts the optimal affinity range towards weaker interactions for enhanced detection.
  • Valency-driven signal enhancement is subject to an affinity threshold.
  • Quantitative insights from this protein-DNA multimer model can guide the design of more complex multivalent systems.