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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
Improving Translational Accuracy02:07

Improving Translational Accuracy

Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...
Proofreading01:43

Proofreading

Overview

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Capturing Common Fragile Site Breaks by Native γH2A.X ChIP
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Published on: January 24, 2025

Information encoded in non-native states drives substrate-chaperone pairing.

Koyeli Mapa1, Satyam Tiwari, Vignesh Kumar

  • 1Proteomics and Structural Biology Unit, CSIR-Institute of Genomics and Integrative Biology, Mall Road, Delhi 110007, India. koyeli.mapa@igib.in

Structure (London, England : 1993)
|July 31, 2012
PubMed
Summary

Protein folding intermediates, often dismissed as in vitro artifacts, can precisely target their cognate chaperones in vivo. This suggests evolution favors sequences encoding intermediates with specific chaperone-binding properties.

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In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
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Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay
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Area of Science:

  • Molecular Biology
  • Protein Folding Dynamics
  • Evolutionary Biochemistry

Background:

  • Proteins often refold in vitro via kinetic folding intermediates.
  • These intermediates are typically considered in vivo by-products lacking translational information.
  • Their role in cellular protein folding remains largely uncharacterized.

Purpose of the Study:

  • To investigate the in vivo relevance of in vitro generated protein folding intermediates.
  • To determine if these intermediates can interact with specific cellular chaperones.
  • To explore the evolutionary implications of intermediate structures in protein folding.

Main Methods:

  • Generation of a test protein's refolding intermediate in vitro.
  • Incubation of the intermediate with a complement of Escherichia coli soluble chaperones.
  • Assessment of chaperone binding specificity using a library of chaperone substrates.
  • Analysis of substrate conformation changes upon cognate chaperone binding.

Main Results:

  • In vitro refolding intermediates successfully identified and bound their cognate chaperones from a complex mixture.
  • Cognate chaperone binding induced unique conformational changes in the non-native substrate.
  • Precise chaperone targeting was maintained at physiological chaperone concentrations.
  • Kinetically trapped intermediates possess sufficient structural information for specific chaperone recognition.

Conclusions:

  • Protein folding intermediates are not merely in vitro artifacts but possess functional roles in vivo.
  • Evolution may favor protein sequences that encode intermediates with specific affinities for cognate chaperones.
  • This finding reframes the understanding of protein folding pathways and evolutionary selection pressures.