Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Formation of Complex Ions

Formation of Complex Ions

A type of Lewis acid-base chemistry involves the formation of a complex ion (or a coordination complex) comprising a central atom, typically a transition metal cation, surrounded by ions or molecules called ligands. These ligands can be neutral molecules like H2O or NH3, or ions such as CN− or OH−. Often, the ligands act as Lewis bases, donating a pair of electrons to the central atom. These types of Lewis acid-base reactions are examples of a broad subdiscipline called coordination...

Ladder Diagrams: Complexation Equilibria

Ladder Diagrams: Complexation Equilibria

Ladder diagrams are useful for evaluating equilibria involving metal-ligand complexes. The vertical scale of the ladder diagram represents the concentration of unreacted or free ligand, pL. The horizontal lines on the scale depict the log of stepwise formation constants for metal-ligand complexes and indicate the dominant species in all the regions.
The formation constant, K1, for the formation of Cd(NH3)2+ complex from cadmium and ammonia is 3.55 × 102. Log K1 (i.e. pNH3) is 2.55, and...

Complexometric Titration: Overview

Complexometric Titration: Overview

Complexometric titration involves the formation of a complex by reacting a metal ion with one or more ligands. A visual indicator often detects the end point of a complexometric titration. It is added to the metal solution before the titration, forming a stable metal–indicator complex and imparting color to the solution. As the titration approaches the equivalence point, the excess of the added ligand displaces the indicator from the metal–indicator complex, releasing the free indicator. The...

You might also read

Related Articles

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

Sort by

Same author

Dysregulation of neurodevelopmental regulatory networks in Anorexia Nervosa: an integrated multi-layered omics analysis.

Frontiers in cell and developmental biology·2026

Same author

HPLC Purification of TRPM8 and Experimental Confirmation of Its Cholesterol Affinity on Synthetic Lipid Raft-like Models.

Life (Basel, Switzerland)·2026

Same author

Liver-specific BAG3 knockout delays chemically induced hepatocellular carcinoma development.

The FEBS journal·2026

Same author

Type-1 Cannabinoid Receptor Promiscuous Coupling: Computational Insights into Receptor-G Protein Interaction Dynamics.

International journal of molecular sciences·2025

Same author

Coordinated epigenetic dysregulation of CNR1 and FAAH genes drives endocannabinoid system dysfunction in anorexia nervosa.

Journal of eating disorders·2025

Same author

EMBL's European Bioinformatics Institute (EMBL-EBI) in 2025.

Nucleic acids research·2025

Search research articles

Related Experiment Video

Updated: Jul 14, 2026

Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers

Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers

Published on: March 21, 2025

Structural characterization of the ceruloplasmin: lactoferrin complex in solution.

Annalaura Sabatucci¹, Patrice Vachette, Vadim B Vasilyev

¹Department of Biomedical Sciences, University of Teramo, Teramo, Italy.

Journal of Molecular Biology

|June 29, 2007

Summary

Human lactoferrin and ceruloplasmin form a 1:1 complex without significant structural changes. Small angle X-ray scattering revealed the complex

More Related Videos

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

Published on: October 15, 2019

Synthesis of Cationized Magnetoferritin for Ultra-fast Magnetization of Cells

Synthesis of Cationized Magnetoferritin for Ultra-fast Magnetization of Cells

Published on: December 13, 2016

Related Experiment Videos

Last Updated: Jul 14, 2026

Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers

Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers

Published on: March 21, 2025

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

Published on: October 15, 2019

Synthesis of Cationized Magnetoferritin for Ultra-fast Magnetization of Cells

Synthesis of Cationized Magnetoferritin for Ultra-fast Magnetization of Cells

Published on: December 13, 2016

Area of Science:

Biochemistry
Structural Biology
Protein Interactions

Background:

Ceruloplasmin is a copper-binding protein in vertebrate plasma belonging to the multicopper oxidase family.
Lactoferrin, an iron-binding protein found in human secretions and leukocytes, binds ferric ions.
Previous studies confirmed in vivo and in vitro interactions between human lactoferrin and ceruloplasmin.

Purpose of the Study:

To investigate the solution conformation of the human lactoferrin/ceruloplasmin complex.
To determine the stoichiometry and structural rearrangements upon complex formation.

Main Methods:

Small angle X-ray scattering (SAXS) was employed to study the complex in solution.
Ab initio structural analysis was performed on the SAXS data.
Rigid-body modeling was used to determine the arrangement of proteins within the complex.

Main Results:

The human lactoferrin/ceruloplasmin complex exhibits a 1:1 stoichiometry.
Complex formation occurs without substantial conformational changes in either protein.
Rigid-body modeling identified two potential families of solutions for the protein arrangement.

Conclusions:

The study elucidates the structural characteristics of the human lactoferrin/ceruloplasmin complex.
SAXS and modeling provide insights into protein-protein interactions in solution.
Further constraints are needed to definitively determine the precise arrangement of the interacting proteins.