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Related Experiment Video

Updated: Jun 22, 2026

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
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Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability

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Salt effects on surface-tethered peptides in solution.

Jun Feng1, Ka-Yiu Wong, Gillian C Lynch

  • 1Department of Biology and Biochemistry, University of Houston, Houston, Texas 77204-5001, USA.

The Journal of Physical Chemistry. B
|June 25, 2009
PubMed
Summary

This study used molecular dynamics simulations to investigate peptide behavior on surfaces. Surface tethering and salt concentration affect peptide thermodynamics and kinetics, slowing conformational changes.

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Peptide diffusion in biomolecular condensates.

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Area of Science:

  • Biophysics
  • Surface Chemistry
  • Computational Biology

Background:

  • Protein and peptide manipulation at liquid-solid interfaces is crucial for biotechnology and detector applications.
  • Understanding the molecular behavior of surface-tethered peptides is essential due to surface inhomogeneity and ion effects.
  • Peptides and proteins exhibit unique thermodynamic and kinetic properties when interacting with hard material surfaces.

Purpose of the Study:

  • To investigate the molecular dynamics of a pentapeptide (RHSVV) tethered to a microarray surface.
  • To analyze the influence of varying salt concentrations (0–1 M NaCl) on tethered and free peptides.
  • To compare the local ion composition around tethered versus free peptides.

Main Methods:

  • Molecular dynamics simulations were employed.

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Last Updated: Jun 22, 2026

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
09:49

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability

Published on: April 2, 2015

Study of Short Peptide Adsorption on Solution Dispersed Inorganic Nanoparticles Using Depletion Method
09:43

Study of Short Peptide Adsorption on Solution Dispersed Inorganic Nanoparticles Using Depletion Method

Published on: April 11, 2020

Glycopeptide Capture for Cell Surface Proteomics
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Glycopeptide Capture for Cell Surface Proteomics

Published on: May 9, 2014

  • Simulations included a pentapeptide tethered to a surface and free in solution.
  • Experiments were conducted across a range of NaCl concentrations (0, 0.14, 0.5, and 1 M).
  • Main Results:

    • Tethered peptide conformational space largely overlaps with free peptides in solution.
    • Surface tethering and salt concentration significantly alter peptide thermodynamics and kinetics.
    • Increased salt concentration and surface tethering reduce the frequency of peptide conformational changes.

    Conclusions:

    • Surface tethering and ionic strength modulate peptide dynamics.
    • The study provides insights into peptide-surface interactions relevant for biosensor and biotechnology design.
    • Conformational dynamics of tethered peptides are sensitive to their ionic environment.