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Related Concept Videos

Protein-protein Interfaces02:04

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 polypeptide...
Protein-Protein Interfaces02:04

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Updated: May 10, 2026

Monitoring Protein Adsorption with Solid-state Nanopores
08:51

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Published on: December 2, 2011

Pressure-induced protein adsorption at aqueous-solid interfaces.

Juny Koo1, Mirko Erlkamp, Sebastian Grobelny

  • 1Fakultät Chemie, TU Dortmund University, D-44221 Dortmund, Germany.

Langmuir : the ACS Journal of Surfaces and Colloids
|June 4, 2013
PubMed
Summary

High pressure can alter protein stability, influencing how strongly proteins like lysozyme bind to surfaces. This study shows high pressure increases protein adsorption by making proteins "softer".

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Insights into the Interactions of Amino Acids and Peptides with Inorganic Materials Using Single-Molecule Force Spectroscopy

Published on: March 6, 2017

Area of Science:

  • Biophysics
  • Protein Science
  • Surface Science

Background:

  • Protein adsorption to interfaces is linked to protein unfolding thermodynamics (ΔG°unf).
  • Hard proteins with high ΔG°unf adsorb weakly, while soft proteins with low ΔG°unf adsorb strongly.
  • Direct experimental evidence linking protein folding stability and interface adsorption under varying conditions is limited.

Purpose of the Study:

  • To provide direct experimental support for the relationship between protein unfolding thermodynamics and interface adsorption.
  • To investigate the effect of high pressure on protein adsorption and structure at solid-aqueous interfaces.
  • To explore the utility of high pressure as a tool for studying protein-interface interactions.

Main Methods:

  • High-pressure total internal reflection fluorescence (HP-TIRF) spectroscopy to measure adsorption.
  • High-pressure neutron reflectometry (HP-NR) to determine protein structure at interfaces.
  • Experiments conducted on lysozyme at hydrophilic and hydrophobic surfaces with varying glycerol concentrations.

Main Results:

  • Protein adsorption to solid surfaces was modulated by applied pressure.
  • Increased pressure led to a greater degree of lysozyme adsorption.
  • Evidence suggests proteins become 'softer' (lower ΔG°unf) at high pressures, enhancing adsorption.

Conclusions:

  • High pressure directly influences the thermodynamics of protein-interface interactions.
  • The study confirms the general rule relating protein unfolding energy and interface affinity.
  • High pressure is a valuable technique for probing protein adsorption and stability at interfaces.