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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...
Extraction: Advanced Methods00:56

Extraction: Advanced Methods

Metal ions can be separated from one another by complexation with organic ligands–the chelating agent– to form uncharged chelates. Here, the chelating agent must contain hydrophobic groups and behave as a weak acid, losing a proton to bind with the metal. Since most organic ligands used in this process are insoluble or undergo oxidation in the aqueous phase, the chelating agent is initially added to the organic phase and extracted into the aqueous phase. The metal-ligand complex is formed in...
Metal-Ligand Bonds02:51

Metal-Ligand Bonds

The hemoglobin in the blood, the chlorophyll in green plants, vitamin B-12, and the catalyst used in the manufacture of polyethylene all contain coordination compounds. Ions of the metals, especially the transition metals, are likely to form complexes.
In these complexes, transition metals form coordinate covalent bonds, a kind of Lewis acid-base interaction in which both of the electrons in the bond are contributed by a donor (Lewis base) to an electron acceptor (Lewis acid). The Lewis acid in...
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Copper metallochaperones.

Nigel J Robinson1, Dennis R Winge

  • 1Institute for Cell and Molecular Biosciences, Medical School, Newcastle University, NE2 4HH, United Kingdom. N.J.Robinson@ncl.ac.uk

Annual Review of Biochemistry
|March 9, 2010
PubMed
Summary
This summary is machine-generated.

Copper metallochaperones are essential proteins that safely deliver copper ions to vital cellular sites, ensuring proper protein function and preventing cellular damage. This review details their role in copper homeostasis and cuproprotein maturation across various organisms.

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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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Quantifying the Binding Interactions Between Cu(II) and Peptide Residues in the Presence and Absence of Chromophores
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Related Experiment Videos

Last Updated: Jun 15, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

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

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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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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Quantifying the Binding Interactions Between Cu(II) and Peptide Residues in the Presence and Absence of Chromophores
11:38

Quantifying the Binding Interactions Between Cu(II) and Peptide Residues in the Presence and Absence of Chromophores

Published on: April 5, 2022

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Copper is an essential trace element crucial for the function of numerous metalloenzymes (cuproproteins).
  • Copper ions (Cu(I) and Cu(II)) are redox-active and can be toxic if not properly managed.
  • Copper metallochaperones are specialized proteins that facilitate the safe transport and delivery of copper ions to target proteins.

Purpose of the Study:

  • To review the current understanding of copper metallochaperone function in cuproprotein maturation.
  • To highlight the diverse cellular locations and roles of cuproproteins requiring copper.
  • To elucidate the mechanisms by which metallochaperones deliver copper without causing cellular damage.

Main Methods:

  • Literature review of existing research on copper metallochaperones and cuproproteins.
  • Analysis of the known cellular pathways involved in copper transport and utilization.
  • Discussion of the proposed mechanisms of copper transfer from chaperones to proteins.

Main Results:

  • Copper is essential for cytochrome oxidase, superoxide dismutase 1 (Sod1), and plastocyanin, located in mitochondria, cytosol, Golgi, chloroplasts, and bacterial periplasm.
  • Copper metallochaperones prevent copper-induced oxidative damage and aberrant binding by escorting ions to specific destinations.
  • Copper ions are released from metallochaperones via ligand substitution upon interaction with their cognate cuproproteins.

Conclusions:

  • Copper metallochaperones play a critical role in cellular copper homeostasis and the biogenesis of essential cuproproteins.
  • Understanding these pathways is vital for comprehending cellular function and potential therapeutic interventions for copper-related disorders.
  • The specific release mechanism ensures precise copper delivery, maintaining cellular redox balance.