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Related Concept Videos

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

17.9K
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...
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Protein Folding01:25

Protein Folding

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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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Structure of Porins01:21

Structure of Porins

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Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
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Protein Organization01:13

Protein Organization

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Overview
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Protein Complex Assembly02:41

Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
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Energy to Drive Translocation01:37

Energy to Drive Translocation

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Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
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Related Experiment Video

Updated: Jun 30, 2025

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
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Structural insights into thermophilic chaperonin complexes.

Zengwei Liao1, Chai C Gopalasingam2, Masafumi Kameya3

  • 1Graduate School of Agricultural and Life Sciences, The University of Tokyo, Bunkyo City, Tokyo 113-8654, Japan.

Structure (London, England : 1993)
|March 16, 2024
PubMed
Summary

Group I chaperonins are essential for protein folding. This study reveals a novel asymmetric football-shaped complex and a unique mechanism for chaperonin-co-chaperonin complex formation using cryo-EM.

Keywords:
GroELSchaperonincryo-EMcryogenic electron microscopyhydrogen-oxidizing bacteriamolecular chaperonesingle particle analysisthermophilic bacteria

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

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Area of Science:

  • Protein homeostasis and molecular chaperones
  • Structural biology of protein complexes
  • Biochemistry of thermophilic bacteria

Background:

  • Group I chaperonins are vital protein folding machines.
  • Dynamic conformational changes in chaperonins are difficult to study.
  • Understanding chaperonin complex turnover is limited.

Purpose of the Study:

  • To investigate the structures of GroES-bound chaperonin complexes.
  • To elucidate dynamic structural variations during complex formation.
  • To understand the mechanism of chaperonin-co-chaperonin complex assembly.

Main Methods:

  • Single-particle cryogenic electron microscopy (cryo-EM).
  • Analysis of chaperonin complexes from Hydrogenophilus thermoluteolus and Hydrogenobacter thermophilus.
  • Inclusion of ATP and AMP-PNP to capture different states.

Main Results:

  • Captured an intermediate state: an asymmetric football-shaped chaperonin complex.
  • Deciphered dynamic structural variations through inter- and intra-subunit communication.
  • Revealed a unique complex formation mechanism involving a second GroES binding to a bullet-shaped complex.

Conclusions:

  • The study provides new insights into chaperonin complex dynamics.
  • A novel mechanism for chaperonin-co-chaperonin complex formation was identified.
  • Structural data advances understanding of protein homeostasis machinery.