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Protein-protein Interfaces

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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...

Protein-Protein Interfaces

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Metal-Ligand Bonds

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Related Experiment Video

Updated: Apr 30, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Interfacial metal coordination in engineered protein and peptide assemblies.

Pamela A Sontz¹, Woon Ju Song¹, F Akif Tezcan¹

¹Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093, United States.

Current Opinion in Chemical Biology

|May 1, 2014

Summary

Metal ions naturally stabilize protein structures and interactions. Researchers are now using coordination chemistry to engineer novel protein and peptide assemblies for advanced applications.

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Area of Science:

Biochemistry
Materials Science
Bioengineering

Background:

Metal ions play crucial roles in natural protein structures and functions, including stabilization and catalysis.
Coordination chemistry offers a powerful toolkit for manipulating metal-ion interactions.

Purpose of the Study:

To provide an overview of metalloprotein/peptide engineering.
To highlight the use of metal ions in designing supramolecular peptide and protein architectures.
To showcase the potential of this emerging field.

Main Methods:

Review of recent literature in metalloprotein/peptide engineering.
Analysis of diverse examples of metal-ion mediated protein assembly.
Exploration of coordination chemistry applications in biomolecular engineering.

Main Results:

Metal ions are versatile tools for stabilizing and directing the assembly of protein and peptide structures.
Coordination chemistry enables precise control over supramolecular architectures.
Emerging examples demonstrate innovative applications in functional materials and biomolecular design.

Conclusions:

Metalloprotein/peptide engineering is a rapidly advancing field with significant potential.
Metal-ion coordination offers a unique strategy for creating complex and functional biomolecular systems.
Future research will likely focus on expanding the scope and applications of these engineered systems.