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Protein-protein Interfaces

Protein-protein Interfaces

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...

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Related Experiment Video

Updated: Nov 6, 2025

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

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

Published on: August 6, 2018

Developments and Ongoing Challenges for Analysis of Surface-Bound Proteins.

Tobias Weidner¹, David G Castner²

¹Department of Chemistry, Aarhus University, 8000 Aarhus C, Denmark;

Annual Review of Analytical Chemistry (Palo Alto, Calif.)

|May 12, 2021

Summary

This summary is machine-generated.

Characterizing surface-bound proteins is crucial for material performance. This study reviews techniques to determine protein structure and concentration on surfaces, enabling better biomaterials and diagnostics.

Keywords:

SFG ToF-SIMS X-ray photoelectron spectroscopy XPS multitechnique analysis protein structure sum frequency generation surface analysis time-of-flight secondary ion mass spectrometry

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Area of Science:

Materials Science
Biophysics
Surface Chemistry

Background:

Proteins at surfaces and interfaces are critical for material function in diagnostics and biomedical devices.
Understanding protein molecular structure (conformation, orientation) and concentration on surfaces is essential for improving material performance.

Purpose of the Study:

To review and describe various experimental and computational techniques for characterizing protein films on material surfaces.
To highlight the capabilities and limitations of current methods for determining the structure of surface-bound proteins.

Main Methods:

Radiolabeling
Surface Plasmon Resonance (SPR)
Quartz Crystal Microbalance with Dissipation (QCM-D)
X-ray Photoelectron Spectroscopy (XPS)
Secondary Ion Mass Spectrometry (SIMS)
Sum Frequency Generation (SFG) Spectroscopy
Computational techniques

Main Results:

A multitechnique approach combining experimental and computational methods is necessary for comprehensive protein film characterization.
Detailed structural information is achievable for small peptides and is being extended to small proteins on surfaces.
Current methods provide significant insight but still lack the resolution for large, complex proteins compared to solution or crystal structures.

Conclusions:

Advanced characterization of surface-bound proteins is vital for developing high-performance biomaterials and diagnostic tools.
While challenges remain, progress in characterizing small peptides and proteins on surfaces is promising.
Future research should focus on enhancing capabilities for detailed structural analysis of surface-bound proteins, especially larger ones.