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 Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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 to...
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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...
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...

You might also read

Related Articles

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

Sort by
Same author

Structural and Functional Characterization of Heterologous Nitrogenase Complexes.

Biochemistry·2026
Same author

Role of Polymer-Protein Interactions in the Dynamics of Polymer-Integrated Protein Crystals.

Journal of the American Chemical Society·2026
Same author

Computational Design of a Highly Stable Dicopper Catechol Oxidase.

Journal of the American Chemical Society·2026
Same author

Design, synthesis, and biological properties exhibited by 1,2,3-triazole based Grp94-selective inhibitors.

European journal of medicinal chemistry·2025
Same author

<i>De Novo</i> Design of a Metalloprotein with a Synthetically Inspired Dinuclear Paddlewheel Coordination Motif.

Journal of the American Chemical Society·2025
Same author

Design of a protein scaffold with a selective, Bi-containing heterodinuclear metal coordination motif.

Journal of inorganic biochemistry·2025

Related Experiment Video

Updated: May 14, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Re-engineering protein interfaces yields copper-inducible ferritin cage assembly.

Dustin J E Huard1, Kathleen M Kane, F Akif Tezcan

  • 1Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California, USA.

Nature Chemical Biology
|January 24, 2013
PubMed
Summary

Scientists engineered a new method, reverse metal-templated interface redesign (rMeTIR), to control protein assembly using metal ions. This allows precise control over protein-protein interactions for studying cellular processes and protein structures.

More Related Videos

Pulldown Assay Coupled with Co-Expression in Bacteria Cells as a Time-Efficient Tool for Testing Challenging Protein-Protein Interactions
07:03

Pulldown Assay Coupled with Co-Expression in Bacteria Cells as a Time-Efficient Tool for Testing Challenging Protein-Protein Interactions

Published on: December 23, 2022

Synthesis of Cationized Magnetoferritin for Ultra-fast Magnetization of Cells
10:23

Synthesis of Cationized Magnetoferritin for Ultra-fast Magnetization of Cells

Published on: December 13, 2016

Related Experiment Videos

Last Updated: May 14, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Pulldown Assay Coupled with Co-Expression in Bacteria Cells as a Time-Efficient Tool for Testing Challenging Protein-Protein Interactions
07:03

Pulldown Assay Coupled with Co-Expression in Bacteria Cells as a Time-Efficient Tool for Testing Challenging Protein-Protein Interactions

Published on: December 23, 2022

Synthesis of Cationized Magnetoferritin for Ultra-fast Magnetization of Cells
10:23

Synthesis of Cationized Magnetoferritin for Ultra-fast Magnetization of Cells

Published on: December 13, 2016

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Engineering

Background:

  • Controlling protein-protein interactions is crucial for understanding cellular dynamics and self-assembling protein structures.
  • Existing methods for controlling protein interactions lack precision and versatility.

Purpose of the Study:

  • To introduce a novel engineering strategy, reverse metal-templated interface redesign (rMeTIR), for chemically controlling protein-protein interactions.
  • To demonstrate the application of rMeTIR in controlling the self-assembly of ferritin protein using copper ions.

Main Methods:

  • Developed the reverse metal-templated interface redesign (rMeTIR) strategy.
  • Engineered the ferritin protein to respond selectively to divalent copper binding for controlled self-assembly.
  • Utilized copper as a structural template to guide ferritin assembly.

Main Results:

  • Successfully rendered ferritin self-assembly controllable by copper binding.
  • Enabled the study of isolated ferritin monomer structure and stability.
  • Demonstrated the critical role of hydrogen bonds in specific cage assembly.
  • Achieved uniform chemical modification of the ferritin cage interior under physiological conditions.

Conclusions:

  • rMeTIR is an effective strategy for creating metal-ion-switchable protein-protein interactions.
  • Copper-templated ferritin assembly provides insights into biological self-assembly mechanisms, similar to RNA templating in virus capsids.
  • This approach opens new avenues for protein engineering and studying dynamic biological systems.