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Molecular Chaperones and Protein Folding03:00

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Related Experiment Video

Updated: Feb 9, 2026

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
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Emerging fields in chaperone proteins: A French workshop.

Elisabetta Mileo1, Marianne Ilbert1, Alessandro Barducci2

  • 1Aix Marseille Univ, CNRS, Laboratoire de Bioénergétique et Ingénierie des Protéines, Marseille, France.

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|June 12, 2018
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Summary

The first French workshop on molecular chaperone proteins and protein folding successfully gathered scientists. Discussions highlighted novel chaperone functions, regulation, and advanced research methods like Cryo-EM and NMR.

Keywords:
AggregationChaperone proteinsFolding/misfoldingMultifunctionalityPlasticityStructural dynamics

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Area of Science:

  • Biochemistry and Molecular Biology
  • Protein Science
  • Cellular Biology

Background:

  • The "Bioénergétique et Ingénierie des Protéines (BIP)" laboratory organized a French workshop focused on molecular chaperones and protein folding.
  • The workshop aimed to unite French researchers in the field of chaperone proteins and protein folding.

Framework:

  • The event facilitated discussions on the diverse roles of molecular chaperones.
  • Exploration of post-translational modifications influencing chaperone activity was a key theme.

Implementation:

  • Discussions covered well-established chaperones like Hsp90, Hsp33, SecB, and GroEL.
  • State-of-the-art methodologies including Cryo-electron microscopy (Cryo-EM), Nuclear Magnetic Resonance (NMR), Electron Paramagnetic Resonance (EPR), and computational modeling were presented.

Implications:

  • The workshop successfully fostered collaboration and knowledge exchange among French scientists.
  • Future workshops are planned to further advance research in chaperone proteins and protein folding within France.