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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
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...
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...
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...

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Related Experiment Video

Updated: May 25, 2026

4D Imaging of Protein Aggregation in Live Cells
08:59

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

Proteome folding and aggregation.

Michele Vendruscolo1

  • 1Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK. mv245@cam.ac.uk

Current Opinion in Structural Biology
|February 10, 2012
PubMed
Summary
This summary is machine-generated.

Maintaining protein solubility requires complex cellular quality control. Impaired mechanisms during aging or stress disrupt protein homeostasis, leading to aggregation and disease.

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Microfluidic Mixers for Studying Protein Folding
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Last Updated: May 25, 2026

4D Imaging of Protein Aggregation in Live Cells
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Published on: April 5, 2013

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
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Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Protein folding at the proteome level involves principles beyond individual molecule behavior.
  • Cellular proteins are often metastable and prone to aggregation due to poor solubility at high expression levels.
  • Maintaining proteome solubility is crucial for cellular function.

Purpose of the Study:

  • To explore the principles governing protein folding at the proteome level.
  • To understand the role of quality control mechanisms in maintaining protein solubility.
  • To investigate the consequences of impaired protein homeostasis.

Main Methods:

  • Review of existing literature on protein folding, aggregation, and quality control.
  • Analysis of cellular mechanisms including molecular chaperones, trafficking, degradation, post-translational modifications, and transcriptional/translational control.
  • Examination of the impact of aging and environmental stress on protein homeostasis.

Main Results:

  • Proteome folding complexity necessitates additional principles beyond single-molecule folding.
  • Quality control mechanisms like chaperones and degradation pathways are essential for protein solubility.
  • Impairment of these mechanisms leads to widespread protein aggregation and disease.

Conclusions:

  • Coordinated quality control is vital for maintaining proteome solubility.
  • Aging and stress compromise these mechanisms, disrupting protein homeostasis.
  • Disrupted protein homeostasis results in uncontrolled aggregation and disease states.