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

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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...
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...
Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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...
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
Evolution of New Traits in Microbes01:24

Evolution of New Traits in Microbes

Microorganisms evolve rapidly due to their large population sizes and short generation times, often exhibiting measurable changes within days under laboratory conditions. Natural selection acts on standing genetic variation, enabling the retention and amplification of beneficial traits that confer fitness advantages in changing environments.Adaptive Pigment Regulation in RhodobacterIn Rhodobacter, a genus of purple non-sulfur bacteria, light-harvesting pigments such as bacteriochlorophyll and...

You might also read

Related Articles

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

Sort by
Same author

Antibiotics stimulate protein transfer to persister cells.

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

Decoupling of global metabolic flux and proteome partitioning in bacteria.

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

The ω subunit stabilizes transcribing RNA polymerase to balance processivity and collision resolution.

bioRxiv : the preprint server for biology·2026
Same author

The phenotypic landscape of the model firmicute Bacillus subtilis.

bioRxiv : the preprint server for biology·2026
Same author

Comprehensive Lineage Tracing Maps the Landscape of Cell Fate Decisions in Mouse Embryogenesis.

bioRxiv : the preprint server for biology·2026
Same author

Short autoinhibitory sequences control phase separation of an essential bacterial transcription termination factor.

The EMBO journal·2026
Same journal

A viral ORFeome library for systems-level genetic dissection of host-pathogen interactions.

Cell·2026
Same journal

Co-option of lysosomal machinery shapes the evolution of the intracellular photosymbiosis supporting coral reefs.

Cell·2026
Same journal

LEF1 and niche factors determine T cell stemness across chronic diseases.

Cell·2026
Same journal

Recurrent patterns of TOP1-mediated neuronal genomic damage shared by major neurodegenerative disorders.

Cell·2026
Same journal

Four-dimensional molecular mapping from a spatial snapshot reveals the dynamics of hair follicle organogenesis.

Cell·2026
Same journal

Whole-cell particle-based digital twin simulations from 4D lattice light-sheet microscopy data.

Cell·2026
See all related articles

Related Experiment Video

Updated: Jul 8, 2026

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 of substrate-optimized GroEL/S chaperonins.

Jue D Wang1, Christophe Herman, Kimberly A Tipton

  • 1Howard Hughes Medical Institute and Department of Cellular and Molecular Pharmacology, University of California, San Francisco 94143, USA.

Cell
|January 1, 2003
PubMed
Summary
This summary is machine-generated.

GroEL/S chaperonins can be engineered for specific protein folding, like green fluorescent protein (GFP). This specialization enhances folding but reduces general substrate capabilities, offering insights into chaperone evolution.

More Related Videos

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

In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity
09:16

In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity

Published on: March 25, 2020

Related Experiment Videos

Last Updated: Jul 8, 2026

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

In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity
09:16

In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity

Published on: March 25, 2020

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Folding

Background:

  • GroEL/S chaperonins are essential molecular machines that assist in protein folding.
  • Their broad substrate range is crucial for cellular function but limits optimization for specific proteins.

Purpose of the Study:

  • To engineer GroEL/S variants with enhanced folding capabilities for a specific substrate, green fluorescent protein (GFP).
  • To investigate the structural and functional basis of chaperonin substrate specificity and plasticity.

Main Methods:

  • Directed evolution using rounds of selection and DNA shuffling.
  • Characterization of GroEL/S variants for altered folding activity and ATPase kinetics.

Main Results:

  • Engineered GroEL/S variants showed significantly enhanced folding of GFP.
  • Structural modifications in optimized chaperonins increased cavity polarity and altered the ATPase cycle.
  • Specialization for GFP folding came at the expense of folding natural substrates.

Conclusions:

  • GroEL/S exhibits remarkable plasticity, allowing for substrate-specific engineering.
  • This engineered plasticity can be leveraged for improved recombinant protein production.
  • The trade-off between specialization and generalization provides evolutionary context for chaperone system development.