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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...
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 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

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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...

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Updated: Jun 28, 2026

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
10:24

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The intramolecular chaperone-mediated protein folding.

Yu-Jen Chen1, Masayori Inouye

  • 1Robert Wood Johnson Medical School, Department of Biochemistry, 675 Hoes Lane, Piscataway, NJ 08854-5635, USA.

Current Opinion in Structural Biology
|November 1, 2008
PubMed
Summary

Intramolecular chaperones are crucial protein sequences aiding folding but not function. These sequences, often N- or C-terminal extensions, are removed post-folding, facilitating proper protein structure formation in vitro and in vivo.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Science

Background:

  • Proteins require specific folding for function.
  • Some proteins utilize internal sequences as intramolecular chaperones.
  • These chaperones are removed after folding.

Purpose of the Study:

  • To review recent findings on intramolecular chaperone-assisted protein folding.
  • To discuss the mechanisms of intramolecular chaperone action.
  • To highlight the importance of these sequences in protein folding.

Main Methods:

  • Literature review of recent studies.
  • Analysis of identified intramolecular chaperone sequences (N-terminal and C-terminal extensions).
  • Discussion of experimental evidence for in vivo and in vitro folding.

Main Results:

  • Intramolecular chaperones are essential for correct protein folding.
  • These sequences are not required for the final protein's function.
  • Evidence supports their role in both cellular and experimental settings.

Conclusions:

  • Intramolecular chaperones are key facilitators of protein folding.
  • Their removal post-folding is a common mechanism.
  • Further research into their precise roles and mechanisms is ongoing.