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

Protein-protein Interfaces02:04

Protein-protein Interfaces

14.9K
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...
14.9K
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

4.6K
4.6K
Protein Complex Assembly02:41

Protein Complex Assembly

17.0K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
17.0K
Ligand Binding Sites02:40

Ligand Binding Sites

15.6K
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...
15.6K
Complexation Equilibria: The Chelate Effect01:19

Complexation Equilibria: The Chelate Effect

1.5K
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...
1.5K
Metal-Ligand Bonds02:51

Metal-Ligand Bonds

25.3K
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...
25.3K

You might also read

Related Articles

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

Sort by
Same author

<i>De novo</i> grafted coiled-coil peptides as p53/<i>h</i>DM2 inhibitors.

RSC chemical biology·2026
Same author

Real-world treatment patterns and outcomes in accelerated and blast-phase myeloproliferative neoplasms: Insights from a large multi-centre cohort analysis in the United Kingdom.

British journal of haematology·2026
Same author

Discovery of SHANK1-PDZ Peptide-Fragment Inhibitors Using a Dynamic Ligation Screening Strategy.

Biochemistry·2026
Same author

Phase 2 study of the lysine-specific demethylase 1 inhibitor bomedemstat for essential thrombocythemia.

Blood advances·2026
Same author

Covalent Peptide-Based N-Myc/Aurora-A Inhibitors Bearing Sulfonyl Fluoride Warheads.

Journal of peptide science : an official publication of the European Peptide Society·2026
Same author

Bora bridges Aurora-A activation and substrate recognition of PLK1.

EMBO reports·2026
Same journal

3-Methyleneazetidine: a versatile building block for functional and post-modifiable polysulfonamides.

Chemical communications (Cambridge, England)·2026
Same journal

Synthesis of divalent galactosyl and fucosyl spiropyran derivatives for the targeted inhibition of bacterial biofilms.

Chemical communications (Cambridge, England)·2026
Same journal

Emergent cytotoxicity and mitochondrial alterations induced by a heterobimetallic Re(I)/Au(I) complex.

Chemical communications (Cambridge, England)·2026
Same journal

Cyanoacetylation of amines <i>via</i> a traceless cyanoacetyl radical: synthetic access to teriflunomide.

Chemical communications (Cambridge, England)·2026
Same journal

Loading layered double hydroxide nanoarray catalysts on a micro-curved substrate for kinetics-favorable water electrolysis reaction.

Chemical communications (Cambridge, England)·2026
Same journal

Bridging <i>in situ</i> measurements and practical conditions through gas-liquid management for CO/CO<sub>2</sub> reduction.

Chemical communications (Cambridge, England)·2026
See all related articles

Related Experiment Video

Updated: Mar 14, 2026

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

10.0K

Correction: Metal complexes as "protein surface mimetics".

Sarah H Hewitt1, Andrew J Wilson1

  • 1School of Chemistry, University of Leeds, Woodhouse Lane, Leeds, LS2 9JT, UK. a.j.wilson@leeds.ac.uk and Astbury Centre for Structural Molecular Biology, University of Leeds, Woodhouse Lane, Leeds, LS2 9JT, UK.

Chemical Communications (Cambridge, England)
|October 7, 2016
PubMed
Summary
This summary is machine-generated.

This correction clarifies details in the original article discussing metal complexes designed to mimic protein surfaces. It ensures accurate representation of these biomimetic compounds in chemical communications.

More Related Videos

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

10.1K
Au-Interaction of Slp1 Polymers and Monolayer from Lysinibacillus sphaericus JG-B53 - QCM-D, ICP-MS and AFM as Tools for Biomolecule-metal Studies
08:29

Au-Interaction of Slp1 Polymers and Monolayer from Lysinibacillus sphaericus JG-B53 - QCM-D, ICP-MS and AFM as Tools for Biomolecule-metal Studies

Published on: January 19, 2016

11.8K

Related Experiment Videos

Last Updated: Mar 14, 2026

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

10.0K
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

10.1K
Au-Interaction of Slp1 Polymers and Monolayer from Lysinibacillus sphaericus JG-B53 - QCM-D, ICP-MS and AFM as Tools for Biomolecule-metal Studies
08:29

Au-Interaction of Slp1 Polymers and Monolayer from Lysinibacillus sphaericus JG-B53 - QCM-D, ICP-MS and AFM as Tools for Biomolecule-metal Studies

Published on: January 19, 2016

11.8K

Area of Science:

  • Coordination Chemistry
  • Biomimetic Chemistry

Background:

  • Protein surface interactions are crucial in biological systems.
  • Developing synthetic mimics is key to understanding and manipulating these interactions.

Purpose of the Study:

  • To correct inaccuracies in the original publication.
  • To ensure precise understanding of metal complexes as protein surface mimetics.

Main Methods:

  • Review and re-evaluation of data presented in the original article.
  • Identification and correction of specific errors in text and figures.

Main Results:

  • Specific errors in the original article have been identified.
  • Corrections are provided to ensure scientific accuracy.

Conclusions:

  • Accurate reporting is essential for scientific progress.
  • This correction maintains the integrity of research on metal complex biomimetics.