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Molecular Chaperones and Protein Folding

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Related Experiment Video

Updated: Mar 27, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Extended functional repertoire for human copper chaperones.

Maria Matson Dzebo, Candan Ariöz, Pernilla Wittung-Stafshede

Biomolecular Concepts

|January 9, 2016

Summary

Copper (Cu) ions are vital for enzymes, but free copper is toxic. Specialized proteins, like the Atox1 chaperone, manage copper transport and signaling, impacting cell growth and disease treatment.

Area of Science:

Biochemistry
Cell Biology
Molecular Biology

Background:

Copper ions (Cu) are essential enzyme cofactors but toxic in free form.
Organisms utilize specialized transport systems and proteins for copper management.
The human cytoplasmic copper chaperone Atox1 delivers Cu to P1B-type ATPases in the Golgi network.

Purpose of the Study:

To elucidate the mechanisms of copper ion transport mediated by cytoplasmic chaperones.
To explore the non-canonical roles of copper chaperones in cellular signaling pathways.
To understand the connection between copper transport and cell regulatory processes for potential therapeutic applications.

Main Methods:

Investigated the structure and function of the copper chaperone Atox1.

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Published on: September 7, 2019

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

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

Published on: September 2, 2019

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Last Updated: Mar 27, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

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Published on: December 16, 2013

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

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

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

Published on: September 2, 2019

Analyzed the interactions between Atox1, CCS, and Cox17 with copper ions and other proteins.

Examined the role of these chaperones in cellular signaling pathways modulating cell growth.

Main Results:

Atox1, a 68-residue ferredoxin-fold protein, binds Cu via a conserved CXXC motif.
Mechanistic details of copper ion transfer between cytoplasmic chaperones (Atox1, CCS, Cox17) have been elucidated.
All three cytoplasmic chaperones interact with signaling pathways affecting cell growth and development.

Conclusions:

Human cells possess a sophisticated network connecting copper transport with cell regulatory processes.
Copper chaperones have dual roles in metal transport and cell signaling.
This knowledge may inform future drug development for cancer and neurodegenerative diseases.