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

Bonding in Metals02:32

Bonding in Metals

Metallic bonds are formed between two metal atoms. A simplified model to describe metallic bonding has been developed by Paul Drüde called the “Electron Sea Model”.
Metallic Solids02:37

Metallic Solids

Metallic solids such as crystals of copper, aluminum, and iron are formed by metal atoms. The structure of metallic crystals is often described as a uniform distribution of atomic nuclei within a “sea” of delocalized electrons. The atoms within such a metallic solid are held together by a unique force known as metallic bonding that gives rise to many useful and varied bulk properties.
All metallic solids exhibit high thermal and electrical conductivity, metallic luster, and malleability. Many...
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...
Ligand Binding Sites02:40

Ligand Binding Sites

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...
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...
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...

You might also read

Related Articles

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

Sort by
Same author

Customizing the structure of minimal TIM barrels to craft efficient de novo enzymes.

Nature chemical biology·2026
Same author

Optimizing Stability in Dynamic Small-Molecule Binding Proteins.

Journal of the American Chemical Society·2025
Same author

The Key to Enzymatic Degradation of Polybutylene Terephthalate (PBT): Influence of Semicrystalline Properties on Degradation.

ChemSusChem·2025
Same author

The 76th Mosbacher Colloquium: AI-driven (r)evolution in structural biology and protein design.

Biological chemistry·2025
Same author

A third type of PETase from the marine Halopseudomonas lineage.

Protein science : a publication of the Protein Society·2025
Same author

Evaluation of Physics-Based Protein Design Methods for Predicting Single Residue Effects on Peptide Binding Specificities.

Journal of computational chemistry·2025
Same journal

The Hedgehog Pathway Effector Smoothened Exhibits Signaling Competency in the Absence of Ciliary Accumulation.

Chemistry & biology·2017
Same journal

DIVERSE System: De Novo Creation of Peptide Tags for Non-enzymatic Covalent Labeling by In Vitro Evolution for Protein Imaging Inside Living Cells.

Chemistry & biology·2015
Same journal

Differential Regulation of Specific Sphingolipids in Colon Cancer Cells during Staurosporine-Induced Apoptosis.

Chemistry & biology·2015
Same journal

Synthetic Peptides as cGMP-Independent Activators of cGMP-Dependent Protein Kinase Iα.

Chemistry & biology·2015
Same journal

Unraveling the B. pseudomallei Heptokinase WcbL: From Structure to Drug Discovery.

Chemistry & biology·2015
Same journal

Vitamin C as Cancer Destroyer, Investigating Sulfhydration, and the Variability in CFTR Interactome.

Chemistry & biology·2015
See all related articles

Related Experiment Video

Updated: May 19, 2026

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

Metals make proteins stick.

Birte Höcker1

  • 1Max Planck Institute for Developmental Biology, 72076 Tübingen, Germany. birte.hoecker@tuebingen.mpg.de

Chemistry & Biology
|March 2, 2010
PubMed
Summary
This summary is machine-generated.

Researchers rationally designed protein interfaces using metal-mediated association. The engineered proteins self-associate without metal, mimicking early protein assembly evolution.

More Related Videos

Standards for Quantitative Metalloproteomic Analysis Using Size Exclusion ICP-MS
09:51

Standards for Quantitative Metalloproteomic Analysis Using Size Exclusion ICP-MS

Published on: April 13, 2016

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

Quantification of Metal Leaching in Immobilized Metal Affinity Chromatography

Published on: January 18, 2020

Related Experiment Videos

Last Updated: May 19, 2026

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

Standards for Quantitative Metalloproteomic Analysis Using Size Exclusion ICP-MS
09:51

Standards for Quantitative Metalloproteomic Analysis Using Size Exclusion ICP-MS

Published on: April 13, 2016

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

Quantification of Metal Leaching in Immobilized Metal Affinity Chromatography

Published on: January 18, 2020

Area of Science:

  • Biochemistry
  • Protein Engineering
  • Evolutionary Biology

Background:

  • Protein-protein interactions are crucial for biological functions.
  • Understanding protein assembly mechanisms is key to protein engineering.
  • Metal ions can mediate and stabilize protein-protein interfaces.

Purpose of the Study:

  • To rationally design self-associating protein interfaces.
  • To investigate metal-mediated protein association as a design strategy.
  • To explore the potential of this approach in mimicking early protein evolution.

Main Methods:

  • Rational design of protein interfaces.
  • Utilizing zinc coordination for initial interface stabilization.
  • Assessing self-association in the absence of metal ions.

Main Results:

  • Successfully designed protein interfaces that self-associate.
  • Demonstrated self-association even after removal of the initial metal ion (zinc).
  • The designed interfaces exhibit stable association without requiring metal cofactors.

Conclusions:

  • Metal-mediated association is a viable strategy for rational protein interface design.
  • Engineered protein interfaces can achieve self-association, mimicking natural evolutionary processes.
  • This approach offers potential for creating novel protein assemblies and understanding protein evolution.