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 Folding01:25

Protein Folding

8.7K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
8.7K
Protein Folding01:22

Protein Folding

112.2K
Overview
112.2K
Protein Folding01:22

Protein Folding

29.7K
29.7K
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

4.8K
Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
4.8K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

14.7K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
14.7K
Proteins: From Genes to Degradation02:11

Proteins: From Genes to Degradation

11.9K
Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA...
11.9K

You might also read

Related Articles

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

Sort by
Same author

Continuous Evolution of Calmodulin for High-Purity Separation of Rare Earth Elements.

Angewandte Chemie (International ed. in English)·2026
Same author

Reducing binding site heterogeneity <i>via</i> truncation of the RTX domain enhances selectivity for rare earth element separation.

Chemical communications (Cambridge, England)·2025
Same author

Mining peptides for mining solutions: evaluation of calcium-binding peptides for rare earth element separations.

Chemical science·2025
Same author

The TRPV1-PKM2-SREBP1 axis maintains microglial lipid homeostasis in Alzheimer's disease.

Cell death & disease·2025
Same author

Neuroprotective Effects of Functionalized Hydrophilic Carbon Clusters: Targeted Therapy of Traumatic Brain Injury in an Open Blast Rat Model.

Biomedicines·2025
Same author

Corrigendum to "Verteporfin combined with ROCK inhibitor promotes the restoration of corneal endothelial cell dysfunction in rats" [Biochem. Pharmacol. 231 (2025) 116641].

Biochemical pharmacology·2025
Same journal

Sustainable Synthesis of Bio-Based Furanic and Aromatic Amines Using an Optimized Whole-Cell Transaminase-Decarboxylase Cascade in E. coli RARE.

Chembiochem : a European journal of chemical biology·2026
Same journal

Composite Dissolvable Microneedle-Enabled Local High-Dose Delivery of Endogenous Thiols for Efficient Allergic Dermatitis Treatment.

Chembiochem : a European journal of chemical biology·2026
Same journal

Revisiting the Radical Quenching Activity of Ebselen Analogues in Homogeneous Phase and In Silico Anti-ferroptotic Activity with Histone Deacetylase.

Chembiochem : a European journal of chemical biology·2026
Same journal

Reaction Optimization for Enzymatic Deconstruction of Industrially Relevant Nylon Composites.

Chembiochem : a European journal of chemical biology·2026
Same journal

Deploying Artificial Metalloenzymes in Complex Environments: Strategies and Applications.

Chembiochem : a European journal of chemical biology·2026
Same journal

Synthetic Ligands of Myeloid C-Type Lectin Receptors.

Chembiochem : a European journal of chemical biology·2026
See all related articles

Related Experiment Video

Updated: Apr 26, 2026

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center
07:11

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center

Published on: September 28, 2022

2.3K

Pyrrolysine-inspired protein cyclization.

Marianne M Lee1, Tomasz Fekner, Jia Lu

  • 1The School of Life Sciences, Centre of Novel Biomaterials, The Chinese University of Hong Kong, Shatin, New Territories, Hong Kong SAR (China). mariannemmlee@cuhk.edu.hk.

Chembiochem : a European Journal of Chemical Biology
|July 22, 2014
PubMed
Summary
This summary is machine-generated.

This study introduces a novel method for creating branched cyclic proteins using pyrrolysine machinery. The technique successfully produced tadpole-like proteins, demonstrating enhanced cellular uptake for RGD peptides.

Keywords:
RGDcyclic peptidesintegrinprotein engineeringpyrrolysine analogues

More Related Videos

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
10:31

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Published on: February 3, 2022

4.3K
Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
11:09

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

9.6K

Related Experiment Videos

Last Updated: Apr 26, 2026

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center
07:11

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center

Published on: September 28, 2022

2.3K
Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
10:31

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Published on: February 3, 2022

4.3K
Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
11:09

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

9.6K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Engineering

Background:

  • Pyrrolysine translational machinery enables site-specific incorporation of non-canonical amino acids.
  • This technology is valuable for in vitro and in vivo biochemical studies.
  • Cyclization of peptides, like RGD, can enhance cellular internalization.

Purpose of the Study:

  • To report the first use of pyrrolysine machinery for producing branched cyclic proteins.
  • To create proteins with a tadpole-like topology.
  • To demonstrate the feasibility of this approach for enhanced cellular uptake.

Main Methods:

  • Fusion of the RGD peptide to the C terminus of an mCherry reporter protein.
  • Utilizing pyrrolysine translational machinery for protein production.
  • Quantifying cellular uptake efficiencies using flow cytometry.

Main Results:

  • Successfully produced branched cyclic proteins with a tadpole-like topology.
  • mCherry-cyclo(RGD) and mCherry-linear(RGD) showed expected cellular uptake efficiencies.
  • Confirmed the feasibility of the cyclization approach.

Conclusions:

  • Pyrrolysine machinery can be effectively used to produce branched cyclic proteins.
  • The tadpole-like cyclization approach is feasible and shows potential utility.
  • This method offers a new strategy for engineering protein function and cellular interaction.