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Related Concept Videos

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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...
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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.
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Related Experiment Video

Updated: Oct 26, 2025

Multiscale Sampling of a Heterogeneous Water/Metal Catalyst Interface using Density Functional Theory and Force-Field Molecular Dynamics
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Multiscale Water Dynamics on Protein Surfaces: Protein-Specific Response to Surface Ions.

Tadeja Janc1,2, Jean-Pierre Korb1, Miha Lukšič2

  • 1Laboratoire PHENIX, CNRS, Sorbonne Université, Paris 75252, France.

The Journal of Physical Chemistry. B
|August 3, 2021
PubMed
Summary
This summary is machine-generated.

This study reveals that salt ions affect water dynamics on protein surfaces differently for lysozyme and bovine serum albumin. The ion-specific effects depend on protein surface geometry, not just ion type.

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Area of Science:

  • Biophysical Chemistry
  • Protein Dynamics
  • Solution Chemistry

Background:

  • Proteins interact with ions in aqueous solutions, with water mediating these interactions.
  • Understanding ion-protein-water dynamics is crucial for biological processes.

Purpose of the Study:

  • To investigate ion-specific water dynamics on protein surfaces using Nuclear Magnetic Resonance Dispersion (NMRD) and theory.
  • To explore how different ions (NaCl, NaI) influence water relaxation rates around hen egg-white lysozyme (LZM) and bovine serum albumin (BSA).

Main Methods:

  • Field-dependent Nuclear Magnetic Resonance Relaxation (NMRD) experiments.
  • Theoretical modeling accounting for non-Lorentzian NMRD profiles and protein surface properties.
  • Analysis of water dynamics on protein surfaces in concentrated solutions.

Main Results:

  • Salt addition caused opposite effects on water relaxation rates for LZM (increase) and BSA (decrease).
  • Ion identity influenced the magnitude of these changes.
  • The developed model successfully reproduced experimental data and explained ion-specific effects through protein surface fractal dimension and water residence times.

Conclusions:

  • Water dynamics at protein surfaces are protein-specific and influenced by ion identity.
  • These effects are linked to the unique geometrical features of protein surfaces.
  • The findings extend beyond simple Hofmeister-style ion ordering.