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 Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

7.4K
Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form...
7.4K
Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

2.6K
2.6K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

8.9K
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...
8.9K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

3.1K
3.1K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

2.7K
2.7K
Turnover Number and Catalytic Efficiency01:19

Turnover Number and Catalytic Efficiency

21.7K
The turnover number of an enzyme is the maximum number of substrate molecules it can transform per unit time. Turnover numbers for most enzymes range from 1 to 1000 molecules per second. Catalase has the known highest turnover number, capable of converting up to 2.8×106 molecules of hydrogen peroxide into water and oxygen per second. Lysozyme has the lowest known turnover number of half a molecule per second.
Chymotrypsin is a pancreatic enzyme that breaks down proteins during digestion....
21.7K

You might also read

Related Articles

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

Sort by
Same author

Nanogravure Printing for PFAS-Free Water-Repellent Textiles with Hierarchical Roughness.

ACS applied materials & interfaces·2026
Same author

Development of UV-Resistant Chitosan/Starch Biofilms Reinforced with Chitosan Nanoparticles for Sustainable Packaging.

Polymers·2026
Same author

Copper-Based Metal-Organic Frameworks for Sustainable Catalysis: Mechanistic Insights, Stability, and Emerging Research Directions.

ACS omega·2026
Same author

Inference for depending competing risks from Marshall-Olikin bivariate Kies distribution under generalized progressive hybrid censoring.

Journal of applied statistics·2025
Same author

Investigating CuO-ZrO<sub>2</sub> Mixed Metal Oxide Nanocomposites for Electrochemical Sensing of Food Colors.

Luminescence : the journal of biological and chemical luminescence·2024
Same author

Chain stretching in brushes favors sequence recognition for nucleobase-functionalized flexible precise oligomers.

Soft matter·2024

Related Experiment Video

Updated: Feb 13, 2026

Direct Force Measurements of Subcellular Mechanics in Confinement using Optical Tweezers
09:56

Direct Force Measurements of Subcellular Mechanics in Confinement using Optical Tweezers

Published on: August 31, 2021

5.6K

Sequence and Surface Confinement Direct Cooperativity in Catalytic Precision Oligomers.

Prakash Chandra1, Alain M Jonas1, Antony E Fernandes1

  • 1Institute of Condensed Matter and Nanosciences, Bio- and Soft Matter , Université Catholique de Louvain , 1348 Louvain-la-Neuve , Belgium.

Journal of the American Chemical Society
|March 17, 2018
PubMed
Summary

Synthetic oligomers with optimized sequences and surface grafting mimic enzyme efficiency. This design enhances catalytic activity by up to 5-fold through confined cooperative pockets, improving molecular assembly functions.

More Related Videos

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
09:34

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Published on: February 6, 2020

8.0K
Confocal Imaging of Confined Quiescent and Flowing Colloid-polymer Mixtures
10:56

Confocal Imaging of Confined Quiescent and Flowing Colloid-polymer Mixtures

Published on: May 20, 2014

12.6K

Related Experiment Videos

Last Updated: Feb 13, 2026

Direct Force Measurements of Subcellular Mechanics in Confinement using Optical Tweezers
09:56

Direct Force Measurements of Subcellular Mechanics in Confinement using Optical Tweezers

Published on: August 31, 2021

5.6K
Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
09:34

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Published on: February 6, 2020

8.0K
Confocal Imaging of Confined Quiescent and Flowing Colloid-polymer Mixtures
10:56

Confocal Imaging of Confined Quiescent and Flowing Colloid-polymer Mixtures

Published on: May 20, 2014

12.6K

Area of Science:

  • Supramolecular chemistry
  • Catalysis
  • Biomimetic design

Background:

  • Enzymes utilize confinement and cooperativity for optimized catalytic activity.
  • Protein sequences precisely fold to preorganize amino acid side chains in binding pockets for synergistic catalysis.

Purpose of the Study:

  • To demonstrate that synthetic precision oligomers can mimic enzyme efficiency.
  • To investigate the role of sequence and spatial arrangement in catalytic activity.

Main Methods:

  • Synthesizing short precision oligomers with specific sequences of catalytic units.
  • Grafting oligomers to a surface to create confined cooperative pockets.
  • Evaluating catalytic activity using the (pyta)Cu/TEMPO/NMI-catalyzed aerobic selective oxidation of alcohols.

Main Results:

  • Optimally sequenced oligomers showed up to 5-fold activity improvement compared to mismatched sequences or free oligomers.
  • Surface grafting and sequence definition induced optimized distribution of catalytic triads.
  • Enhanced catalytic efficiency resulted from matched interchain interactions in the surface-confined system.

Conclusions:

  • Sequence definition and surface grafting create confined cooperative pockets that enhance catalytic efficiency.
  • This approach offers a new paradigm for designing molecular assemblies with enzyme-like precision.
  • The study highlights the importance of interchain interactions in surface-confined catalytic systems.