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Protein Organization01:24

Protein Organization

8.4K
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
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Metal-Ligand Bonds02:51

Metal-Ligand Bonds

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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...
22.9K
Proteomics01:33

Proteomics

8.9K
A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...
8.9K
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
5.2K
Ligand Binding Sites02:40

Ligand Binding Sites

14.5K
Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
14.5K
Protein Folding01:25

Protein Folding

10.1K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
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Related Experiment Video

Updated: Nov 20, 2025

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
11:04

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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Recent advances in protein metalation: structural studies.

Antonello Merlino1

  • 1Department of Chemical Sciences, University of Naples Federico II, Complesso Universitario di Monte Sant'Angelo, Via Cintia, I-80126, Napoli, Italy. antonello.merlino@unina.it.

Chemical Communications (Cambridge, England)
|January 19, 2021
PubMed
Summary

Protein metalation, the binding of metal compounds to proteins, is vital for drug action and designing new metalloenzymes. Structural studies reveal diverse binding mechanisms and flexibility in metal-protein adducts.

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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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Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
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Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Medicinal Chemistry

Background:

  • Protein metalation forms adducts between metal compounds and proteins.
  • This process is critical for understanding metal-based drug mechanisms, toxicity, and designing artificial metalloenzymes and drug delivery systems.

Purpose of the Study:

  • To review recent structural advances in metal compound-protein recognition.
  • To analyze the binding characteristics of various metal-protein adducts.

Main Methods:

  • Analysis of structural data for protein adducts with Pt, Au, Ru, Re, Pd, Ir, Os, Rh, and Pt-As.
  • Application of Hard and Soft Acids and Bases (HSAB) principles.

Main Results:

  • Metal compounds bind proteins through non-covalent interactions or coordination to side chains after ligand release.
  • Protein binding can induce reduction/oxidation, altering the metal's coordination sphere and compound stability.
  • Binding sites vary, showing preferences for specific side chains governed by HSAB principles, with adaptable binding site numbers and types.
  • Metal-protein adducts maintain flexibility and reactivity.

Conclusions:

  • Structural insights illuminate the complex mechanisms of protein metalation.
  • Understanding these interactions is key for developing targeted metallodrugs and biomaterials.