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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: Jun 6, 2026

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

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

Protein folding in the cell: challenges and progress.

Anne Gershenson1, Lila M Gierasch

  • 1Department of Biochemistry & Molecular Biology, University of Massachusetts, Amherst, MA 01003, USA. gierasch@biochem.umass.edu

Current Opinion in Structural Biology
|November 30, 2010
PubMed
Summary

Protein folding in cells differs greatly from lab studies due to crowding and other factors. Recent research explores these in-cell protein folding challenges and new methods to study them.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • In vitro protein folding studies use dilute solutions, which do not reflect the cellular environment.
  • The cellular interior is crowded, compartmentalized, and spatially inhomogeneous.
  • Key factors like macromolecular crowding, hindered diffusion, and molecular chaperones influence protein folding in vivo.

Purpose of the Study:

  • To review recent research on protein folding within the cellular environment.
  • To highlight differences between in vitro and in-cell protein folding.
  • To discuss challenges and advances in studying protein folding in cells.

Main Methods:

  • Review of recent scientific literature on in-cell protein folding.
  • Discussion of technical obstacles in characterizing protein folding in vivo.
  • Highlighting methodological advances such as fluorescence imaging and genetic screens.

Main Results:

  • Protein folding in cells is significantly impacted by factors absent in dilute in vitro conditions.
  • Macromolecular crowding, hindered diffusion, cotranslational folding, and molecular chaperones are critical in-cell considerations.
  • New techniques are emerging to overcome technical challenges in studying cellular protein folding.

Conclusions:

  • Understanding protein folding in the cellular context requires considering unique intracellular factors.
  • Methodological innovations are crucial for advancing the study of in-cell protein folding.
  • Future research should focus on bridging the gap between in vitro and in vivo protein folding.