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Related Concept Videos

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
Protein Folding01:22

Protein Folding

Overview
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

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...
Improving Translational Accuracy02:07

Improving Translational Accuracy

Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...

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Related Experiment Video

Updated: Jun 14, 2026

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

Cotranslational folding increases GFP folding yield.

Krastyu G Ugrinov1, Patricia L Clark

  • 1Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA.

Biophysical Journal
|April 8, 2010
PubMed
Summary
This summary is machine-generated.

Cotranslational folding, where proteins fold during synthesis, dramatically increases the yield of correctly folded GFP compared to post-translational folding. This suggests cotranslational folding minimizes protein aggregation.

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Last Updated: Jun 14, 2026

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

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Coupled Assays for Monitoring Protein Refolding in Saccharomyces cerevisiae
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Coupled Assays for Monitoring Protein Refolding in Saccharomyces cerevisiae

Published on: July 9, 2013

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Protein Folding

Background:

  • Proteins fold into specific three-dimensional structures within cells.
  • Cotranslational folding occurs as polypeptide chains are synthesized by ribosomes.
  • The constraints of cotranslational folding may impact protein folding outcomes.

Purpose of the Study:

  • To investigate if cotranslational folding constraints influence the balance between productive folding and aggregation.
  • To compare the folding yield of nascent polypeptide chains versus full-length denatured chains.

Main Methods:

  • Isolation of polyribosomes from Escherichia coli expressing Green Fluorescent Protein (GFP).
  • Analysis of nascent chain length distribution.
  • Calculation of folding yield upon ribosome release versus dilution from denaturant.

Main Results:

  • A significantly higher yield of native fluorescent GFP was observed upon ribosome release of nascent chains.
  • This yield was higher compared to folding of equivalent concentrations of full-length, chemically denatured GFP.

Conclusions:

  • Cotranslational folding enhances the efficiency of achieving the native structure for proteins like GFP.
  • Correct first-time folding during cotranslational synthesis can prevent aggregation and ensure lifelong native structure population.