Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

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.
These groups modify specific amino acids in a protein.
Complexation Equilibria: Factors Influencing Stability of Complexes01:09

Complexation Equilibria: Factors Influencing Stability of Complexes

In complexation reactions, metal cations are the electron pair acceptors, and the ligands are the electron pair donors. The stability of the metal complexes depends primarily on the complexing ability of the central metal ion and the nature of the ligands. Generally, the complexing ability of the metal ion depends on the size and charge of the ion. As the metal ion size increases, the stability of the metal complexes decreases, provided that the valency of the metal ion and the ligands remain...
EDTA: Auxiliary Complexing Reagents01:26

EDTA: Auxiliary Complexing Reagents

EDTA titrations are usually carried out in highly basic conditions, where the fully deprotonated form of EDTA, Y4−, actively complexes with the free metal ions in the solution. Several metal ions precipitate as hydrous oxide (hydroxides, oxides, or oxyhydroxides) under these conditions, lowering the concentration of free metal ions in the solution. For this reason, auxiliary complexing agents or ligands such as ammonia, tartrate, citrate, or triethanolamine are used in EDTA titrations to...
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...
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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

A Scorpion Venom-Derived Peptide M6 Endowed with Anti-Aging Ability via Enhanced Antioxidant Activity in Cells, <i>Caenorhabditis elegans</i> and Mouse Models.

International journal of biological sciences·2026
Same author

Endosomal escape and cytosolic delivery of cell-penetrating peptide conjugates.

Bioorganic & medicinal chemistry·2026
Same author

Contact Parallel Cascade Selection Molecular Dynamics (cPaCS-MD) for Accurate In Silico Prediction of Peptide Binding Free Energy.

Journal of chemical information and modeling·2025
Same author

Cell-penetrant peptides as novel inhibitors of the interaction of coatomer protein COPB2/RACK2 with protein kinase Cε and cargo proteins.

Biochimica et biophysica acta. Molecular cell research·2025
Same author

<i>Toxicon</i> and <i>Toxicon: X</i> - Editorial transitions and future directions in 2025.

Toxicon: X·2025
Same author

Toxicon and Toxicon: X - Editorial Transitions and Future Directions in 2025.

Toxicon : official journal of the International Society on Toxinology·2025
Same journal

Reshaping the glycocalyx: the SULF extracellular endosulfatases as molecular editors of heparan Sulfate.

The Biochemical journal·2026
Same journal

Mechanistic insights into acetylated histone recognition by the CECR2 bromodomain.

The Biochemical journal·2026
Same journal

Nanobodies against Plasmodium adhesins that block receptor engagement and malaria parasite invasion.

The Biochemical journal·2026
Same journal

Persistence without turnover: the RhoG G12E mutant highlights the role of nucleotide cycling in RhoG signaling.

The Biochemical journal·2026
Same journal

Alternative Splicing of Rice Chloroplastic CuZn Superoxide Dismutase, OsCSD2: Impact on expression and protein characteristics.

The Biochemical journal·2026
Same journal

Difference and similarity between the ubiquitous secretory pathway Ca2+-ATPases, SERCA2b, and SPCA1a.

The Biochemical journal·2026
See all related articles

Related Experiment Video

Updated: Jul 3, 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

Tyrosine modification enhances metal-ion binding.

Graham S Baldwin1, Michael F Bailey, B Philip Shehan

  • 1The University of Melbourne Department of Surgery, Austin Health, Heidelberg, Victoria 3084, Australia. grahamsb@unimelb.edu.au

The Biochemical Journal
|July 19, 2008
PubMed
Summary
This summary is machine-generated.

Tyrosine modification, like sulfation or phosphorylation, enhances metal-ion binding affinity in peptides such as cholecystokinin (CCK). This suggests metal ions may directly regulate cellular signaling pathways.

More Related Videos

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

Published on: September 7, 2019

Quantification of Metal Leaching in Immobilized Metal Affinity Chromatography
05:35

Quantification of Metal Leaching in Immobilized Metal Affinity Chromatography

Published on: January 17, 2020

Related Experiment Videos

Last Updated: Jul 3, 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
11:04

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

Published on: September 7, 2019

Quantification of Metal Leaching in Immobilized Metal Affinity Chromatography
05:35

Quantification of Metal Leaching in Immobilized Metal Affinity Chromatography

Published on: January 17, 2020

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Metalloprotein

Background:

  • Tyrosine sulfation and phosphorylation are critical protein modifications.
  • Growth-factor receptors often possess tyrosine phosphorylation capabilities.
  • Cholecystokinin (CCK), existing in sulfated and unsulfated forms, serves as a model peptide.

Purpose of the Study:

  • To investigate the impact of tyrosine modification on metal-ion binding.
  • To compare metal-ion binding characteristics of modified and unmodified CCK(8).

Main Methods:

  • Utilized cholecystokinin (CCK(8)) as a model peptide.
  • Employed absorbance and fluorescence spectroscopy for Fe(3+) binding studies.
  • Used a Ca(2+)-selective electrode for Ca(2+) binding measurements.

Main Results:

  • Tyrosine sulfation/phosphorylation increased Fe(3+) binding stoichiometry to 2, with affinity largely unaffected.
  • Phosphorylated CCK(8) bound two Ca(2+) ions, while unmodified/sulfated CCK(8) bound one with lower affinity.
  • Pre-binding of Ca(2+), Zn(2+), or Bi(3+) to phosphorylated CCK(8) enhanced subsequent Fe(3+) binding signal.

Conclusions:

  • Tyrosine modification can enhance metal-ion binding affinity to peptides.
  • Metal ions may play a direct role in regulating peptide-mediated signaling pathways.