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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...
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...
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

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In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
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Published on: September 2, 2019

Chaperonins: two rings for folding.

Hugo Yébenes1, Pablo Mesa, Inés G Muñoz

  • 1Centro Nacional de Biotecnología (CNB-CSIC), Campus de la Universidad Autónoma de Madrid, Darwin 3, 28049 Madrid, Spain.

Trends in Biochemical Sciences
|July 5, 2011
PubMed
Summary

Group II chaperonins, including the complex eukaryotic cytosolic CCT, are less understood than Group I. Recent structural studies reveal key differences in their functional mechanisms and molecular rearrangements.

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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Published on: June 7, 2018

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Chaperonins are essential molecular chaperones present across diverse life forms, including Eubacteria, Archaea, and eukaryotic organelles and cytosol.
  • They share a conserved structure and fundamental mechanism for protein folding assistance.
  • Group I chaperonins are well-characterized, but Group II chaperonins remain less understood.

Purpose of the Study:

  • To elucidate the distinct structural and mechanistic features of Group II chaperonins compared to Group I.
  • To highlight the unique aspects of the eukaryotic cytosolic chaperonin (CCT).

Main Methods:

  • Analysis of recent crystallographic structures.
  • Interpretation of electron microscopy data.

Main Results:

  • New structural insights reveal significant differences in the functional cycle of Group II chaperonins.
  • Key distinctions lie in the molecular rearrangements occurring during the chaperonin's mechanism.
  • The eukaryotic cytosolic CCT exhibits unique characteristics within the Group II family.

Conclusions:

  • Group II chaperonins, particularly CCT, possess unique mechanisms distinct from Group I chaperonins.
  • Structural studies are crucial for understanding the specialized functions of complex chaperonins like CCT.