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Related Concept Videos

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...
The Significance of Membrane Transport01:44

The Significance of Membrane Transport

The transport of solutes across the cell membrane is essential for metabolic processes, like maintaining cell size and volume, generating the action potential, exchanging nutrients and gases, etc. Membrane transport can be either passive or active. It can be simple diffusion, facilitated, or mediated transport aided by transport proteins such as transporters and channels.
Transporters facilitate either an active or passive movement of solutes. They can allow a single-molecule transport down its...
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
Receptor-mediated Endocytosis01:20

Receptor-mediated Endocytosis

Receptor-mediated endocytosis is when bulk amounts of specific molecules are imported into a cell after binding to cell surface receptors. The molecules bound to these receptors are taken into the cell through inward folding of the cell surface membrane, which is eventually pinched off into a vesicle within the cell. Structural proteins, such as clathrin, coat the budding vesicle.
Clathrin-Mediated Endocytosis of LDL
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Nuclear Protein Sorting01:34

Nuclear Protein Sorting

Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
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Related Experiment Video

Updated: Jun 13, 2026

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

Molecular recognition in copper trafficking.

Lucia Banci1, Ivano Bertini, Kathleen S McGreevy

  • 1Department of Chemistry, University of Florence, Fiorentino, Italy. banci@cerm.unifi.it

Natural Product Reports
|May 6, 2010
PubMed
Summary
This summary is machine-generated.

Cellular systems precisely manage essential metal ions like copper. Imbalances in copper concentration and distribution can cause cell damage, highlighting the importance of molecular recognition mechanisms.

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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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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
  • Metallomics

Background:

  • Cellular systems utilize diverse molecular mechanisms for metal ion homeostasis.
  • Proper handling of essential yet toxic metals, such as copper, is critical for cell survival.
  • Dysregulation of intracellular metal concentration and distribution can lead to pathological conditions.

Purpose of the Study:

  • To explore the molecular mechanisms governing metal ion handling in cellular systems.
  • To understand the role of copper homeostasis in cellular health and disease.
  • To investigate the interplay between metal coordination chemistry and protein interactions in molecular recognition.

Main Methods:

  • Literature review on cellular metal ion transport and binding.
  • Analysis of research linking metal dyshomeostasis to cellular pathology.
  • Examination of studies on copper's dual role as essential nutrient and toxin.
  • Review of molecular recognition principles in metalloprotein interactions.

Main Results:

  • Cellular metal ion management ranges from simple ion export to complex eukaryotic systems.
  • Copper's essentiality is balanced by its potential toxicity, requiring strict intracellular control.
  • Molecular recognition is finely tuned by the interplay of metal coordination chemistry and protein-protein interactions.

Conclusions:

  • Effective cellular metal ion homeostasis is fundamental for life.
  • Precise control over copper levels is vital to prevent cellular dysfunction and disease.
  • The intricate coordination between metal chemistry and protein interactions governs cellular metal recognition.