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

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...
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
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...
Conservation of Protein Domains02:26

Conservation of Protein Domains

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Protein Folding01:25

Protein Folding

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...
Protein Folding01:22

Protein Folding

Overview

You might also read

Related Articles

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

Sort by
Same author

An engineered closed-shell, two-component, 480-subunit nucleocapsid.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Analyses of Recent Hit-Finding Campaigns for Difficult Targets Provides Guidance for Informed Integrated Hit Discovery.

ACS medicinal chemistry letters·2026
Same author

Identification of overoxidizing and non-overoxidizing NAD-dependent methanol dehydrogenases and implications for synthetic methylotrophy.

Nature communications·2025
Same author

Computational design of cysteine proteases.

bioRxiv : the preprint server for biology·2025
Same author

Computational design of metalloproteases.

bioRxiv : the preprint server for biology·2025
Same author

Computational design of metallohydrolases.

Nature·2025
Same journal

Erratum for the Research Article "Detecting supramolecular organic nanoparticles during heat wave".

Science (New York, N.Y.)·2026
Same journal

Local signals, systemic decline.

Science (New York, N.Y.)·2026
Same journal

The mechanics of liver regeneration.

Science (New York, N.Y.)·2026
Same journal

Computing in a memory with physics.

Science (New York, N.Y.)·2026
Same journal

Retraction.

Science (New York, N.Y.)·2026
Same journal

Making time.

Science (New York, N.Y.)·2026
See all related articles

Related Experiment Video

Updated: Jun 4, 2026

Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification
10:21

Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification

Published on: November 16, 2016

Directed evolution of a protein container.

Bigna Wörsdörfer1, Kenneth J Woycechowsky, Donald Hilvert

  • 1Laboratory of Organic Chemistry, Eidgenössische Technische Hochschule (ETH) Zürich, 8093 Zürich, Switzerland.

Science (New York, N.Y.)
|February 5, 2011
PubMed
Summary
This summary is machine-generated.

Researchers engineered protein nanocompartments to safely contain toxic enzymes like HIV protease within cells. This method improved host cell growth and led to the development of enhanced capsids with higher enzyme-loading capacity for biotechnological applications.

More Related Videos

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
13:30

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes

Published on: November 7, 2012

Directed Evolution Method in Saccharomyces cerevisiae: Mutant Library Creation and Screening
10:50

Directed Evolution Method in Saccharomyces cerevisiae: Mutant Library Creation and Screening

Published on: April 1, 2016

Related Experiment Videos

Last Updated: Jun 4, 2026

Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification
10:21

Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification

Published on: November 16, 2016

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
13:30

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes

Published on: November 7, 2012

Directed Evolution Method in Saccharomyces cerevisiae: Mutant Library Creation and Screening
10:50

Directed Evolution Method in Saccharomyces cerevisiae: Mutant Library Creation and Screening

Published on: April 1, 2016

Area of Science:

  • Synthetic biology
  • Biotechnology
  • Protein engineering

Background:

  • Enzyme confinement in protein nanocompartments offers a strategy for controlling cellular catalytic activity.
  • Toxic enzymes, such as HIV protease, pose challenges for intracellular production due to host toxicity.

Purpose of the Study:

  • To develop a method for sequestering toxic enzymes within engineered protein capsids.
  • To improve capsid properties through directed evolution for enhanced enzyme containment and host protection.
  • To explore the potential of engineered nanocompartments for biotechnological applications in living cells.

Main Methods:

  • Utilized an electrostatically based tagging system for protein encapsulation.
  • Engineered lumazine synthase capsids to sequester HIV protease in Escherichia coli.
  • Employed directed evolution, involving mutagenesis and selection, to enhance capsid performance.

Main Results:

  • Successfully sequestered toxic HIV protease within engineered lumazine synthase capsids.
  • Achieved a 5- to 10-fold increase in capsid loading capacity after four rounds of evolution.
  • Demonstrated efficient host cell growth despite high intracellular concentrations of HIV protease.
  • Identified mutations increasing net negative charge on the capsid's luminal surface, enhancing electrostatic interactions.

Conclusions:

  • Engineered protein nanocompartments provide a robust platform for managing toxic enzyme activity within cells.
  • Directed evolution can yield improved capsids with significantly enhanced enzyme-loading capacity.
  • These advanced nanocompartments hold promise for diverse biotechnological applications in living systems.