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Related Concept Videos

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...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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Protein Denaturation01:28

Protein Denaturation

The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
EDTA: Chemistry and Properties01:22

EDTA: Chemistry and Properties

Polydentate ligands are most widely used in complexometric titrations because they form more stable complexes with the metal ions than mono- or bidentate ligands due to the chelate effect. Examples of polydentate ligands are ethylenediaminetetraacetic acid (EDTA), crown ethers, and cryptands. The most important feature of optimal polydentate ligands is the ability to form 1:1 complexes in a single-step process. Amino carboxylic acid derivatives are frequently used as complexing agents. EDTA is...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Complexation Equilibria: The Chelate Effect01:19

Complexation Equilibria: The Chelate Effect

In complexation reactions, metal atoms or cations interact with ligands to form donor-acceptor adducts called metal complexes. Ligands that bind through one donor site are monodentate, ligands with two donor sites are bidentate, and those with more than two donor sites are polydentate ligands. For example, ethylene diamine is a bidentate ligand that binds through two nitrogen donor atoms, forming a five-membered ring. EDTA is a polydentate ligand that binds through four oxygen and two nitrogen...

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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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Metal ion-mediated DNA-protein interactions.

Barbara Zambelli1, Francesco Musiani, Stefano Ciurli

  • 1Department of Agro-Environmental Science and Technology, University of Bologna, Bologna, Italy. barbara.zambelli@unibo.it

Metal Ions in Life Sciences
|January 3, 2012
PubMed
Summary

Organisms adapt to environmental changes by evolving specialized metal-sensing proteins. These metal-responsive regulators control cellular metal levels and gene expression, crucial for metal homeostasis.

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Quantitative Detection of DNA-Protein Crosslinks and Their Post-Translational Modifications

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Area of Science:

  • Biochemistry and Molecular Biology
  • Environmental Adaptation
  • Genetics

Background:

  • Environmental changes drive evolution of metal ion sensing in organisms.
  • Organisms possess specific metal-responsive transcriptional regulators to manage intracellular metal content.
  • Understanding metal-protein and protein-DNA interactions is key to deciphering metal homeostasis networks.

Purpose of the Study:

  • To elucidate the molecular mechanisms of protein-metal ion recognition.
  • To explain how metal binding is transduced into transcriptional output.
  • To review structural insights into metal-responsive transcriptional regulators.

Main Methods:

  • Analysis of structural information on metal-responsive transcriptional regulators.
  • Examination of metal-protein and protein-DNA interactions.
  • Review of recent advances in understanding metal ion selection and allosteric responses.

Main Results:

  • Metal ion binding to proteins alters their DNA interactions, influencing gene expression.
  • Specific structural features enable metal-responsive regulators to choose particular metal ions.
  • Allosteric regulation allows these proteins to respond to effector binding.

Conclusions:

  • Metal-driven differentiation has shaped cellular metal sensing and utilization.
  • Structural studies provide a basis for understanding metal-protein and protein-DNA recognition.
  • Further research on these regulators advances our knowledge of metal homeostasis and gene regulation.