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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...
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...
Aquaporins01:25

Aquaporins

Aquaporins or AQPs are a family of integral membrane proteins whose primary function is to transport water, while some called aquaglyceroporins also transport glycerol. In addition, aquaporins have also been suspected to be involved in transporting volatile substances, such as carbon dioxide and ammonia, across membranes. Such AQPs that act as gas channels are often highly expressed in cells involved in the gaseous exchange, such as red blood cells, epithelial cells, and pulmonary capillaries.
Protein Folding01:22

Protein Folding

Overview
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...

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Updated: Jul 2, 2026

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
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Published on: October 23, 2016

A role for confined water in chaperonin function.

Jeremy L England1, Del Lucent, Vijay S Pande

  • 1James H. Clark Center, S297, Stanford University, Stanford, California 94305, USA.

Journal of the American Chemical Society
|August 20, 2008
PubMed
Summary

Bacterial chaperonins like GroEL help proteins fold. Their folding assistance is linked to how well their inner surfaces attract water, offering new insights into confined water behavior during protein folding.

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Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
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In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
08:58

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

Published on: September 2, 2019

Area of Science:

  • Molecular Biology
  • Biophysics
  • Computational Chemistry

Background:

  • Chaperonins are protein complexes that assist in protein folding.
  • The precise mechanism by which chaperonins accelerate protein folding remains largely unknown.
  • Understanding protein folding is crucial for comprehending cellular function and disease.

Purpose of the Study:

  • To investigate the mechanism of protein folding facilitation by chaperonins.
  • To explore the role of the chaperonin's internal environment in protein folding.
  • To correlate chaperonin activity with the properties of water confined within its structure.

Main Methods:

  • All-atom molecular dynamics simulations were employed to model the behavior of chaperonins.
  • Experimental assays measuring the activity of the bacterial chaperonin GroEL were conducted.
  • Data from simulations and experiments were integrated to analyze structure-function relationships.

Main Results:

  • A strong correlation was identified between chaperonin folding-facilitating activity and the affinity of its interior surface for water.
  • The study provides evidence that the interaction of confined water with the chaperonin surface is a key factor.
  • Simulation results align with experimental observations of GroEL activity.

Conclusions:

  • Chaperonin-mediated protein folding is significantly influenced by the hydrophobic/hydrophilic properties of its internal cavity.
  • The behavior of water confined within chaperonins plays a critical role in accelerating protein folding.
  • This research proposes a novel perspective on the function of confined water in biological systems, relevant to in vivo protein folding.