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

11.7K
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...
11.7K
Protein Folding01:22

Protein Folding

128.6K
Overview
128.6K
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

5.3K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
5.3K
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

18.0K
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...
18.0K
Termination of Translation01:44

Termination of Translation

28.1K
The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
28.1K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

20.0K
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...
20.0K

You might also read

Related Articles

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

Sort by
Same author

Complete enzyme clustering enhances coenzyme Q biosynthesis via substrate channeling.

Nature communications·2026
Same author

Biophysical fitness landscape design traps viral evolution.

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

Chaperonin recognition of protein dynamics drives drug resistance.

bioRxiv : the preprint server for biology·2026
Same author

Co-targeting Metabolic Neighbours Constraints Bacterial Adaptive Evolution.

bioRxiv : the preprint server for biology·2026
Same author

CASPULE: A computational tool to study sticker spacer polymer condensates.

PLoS computational biology·2026
Same author

Evolutionary dynamics under phenotypic uncertainty.

bioRxiv : the preprint server for biology·2026

Related Experiment Video

Updated: Feb 20, 2026

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
08:59

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

Published on: February 12, 2019

12.0K

Evidence of evolutionary selection for cotranslational folding.

William M Jacobs1, Eugene I Shakhnovich2

  • 1Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138.

Proceedings of the National Academy of Sciences of the United States of America
|October 27, 2017
PubMed
Summary

Evolutionary selection favors cotranslational folding, where proteins fold on the ribosome. This study reveals conserved gene regions with slow translation, suggesting selection optimizes folding intermediates for efficiency.

Keywords:
cotranslational foldingfree-energy landscapesprotein-folding intermediatessynonymous codon usage

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

3.5K
Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
10:09

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

Published on: April 28, 2011

18.8K

Related Experiment Videos

Last Updated: Feb 20, 2026

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
08:59

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

Published on: February 12, 2019

12.0K
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

3.5K
Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
10:09

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

Published on: April 28, 2011

18.8K

Area of Science:

  • Molecular Biology
  • Evolutionary Biology
  • Biophysics

Background:

  • Recent studies suggest proteins can fold during translation on the ribosome.
  • The extent and impact of fitness effects from cotranslational folding are not fully understood.

Purpose of the Study:

  • To investigate evolutionary selection for cotranslational folding.
  • To identify specific gene regions under selection related to this process.

Main Methods:

  • Genome-wide analysis of Escherichia coli genes.
  • Statistical identification of loci enriched in slowly translated codons and conserved across species.
  • Comparison with domain boundaries and a native-centric cotranslational folding model.

Main Results:

  • Identified conserved gene loci with slow translation rates, not solely explained by domain boundaries.
  • Found that predicted cotranslational folding intermediates correlate with the majority of these loci.
  • Demonstrated evidence for selection optimizing translation rates at specific gene locations.

Conclusions:

  • Cotranslational folding is under significant evolutionary selection.
  • Selection appears to optimize folding intermediates, which can be smaller than protein domains.
  • Biological self-assembly efficiency is influenced by kinetic factors during translation, not just thermodynamics.