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The ionic association is the association of oppositely charged ions in an electrolyte solution to form ion pairs. Bjerrum defined ion pairs as two oppositely charged ions whose electrostatic attraction exceeds the thermal energy of the system, typically expressed as 2kT. Electrostatic attraction depends on ionic charge, separation distance, and the dielectric constant of the medium. Thermal energy, represented by kT, reflects the tendency of ions to move independently due to molecular motion.
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Related Experiment Video

Updated: Apr 16, 2026

Quantifying the Binding Interactions Between CuII and Peptide Residues in the Presence and Absence of Chromophores
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Counterion effects in protein nanoparticle electrostatic binding: a theoretical study.

Goutam Ghosh1

  • 1UGC-DAE Consortium for Scientific Research, Mumbai Centre, Trombay, Mumbai 400085, India.

Colloids and Surfaces. B, Biointerfaces
|March 3, 2015
PubMed
Summary
This summary is machine-generated.

Counterions diffusing into proteins bound to nanoparticles cause partial unfolding. Increased counterion diffusion and polarizability decrease protein folding energy, impacting protein conformation.

Keywords:
Counterion effectsDipole and induced-ion interactionsIon solvation in waterProtein folding energyProtein–nanoparticle electrostatic binding

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Area of Science:

  • Biophysics
  • Nanotechnology
  • Computational Chemistry

Background:

  • Proteins electrostatically bound to functionalized nanoparticles can undergo conformational changes.
  • Understanding these changes is crucial for applications in drug delivery and biosensing.

Purpose of the Study:

  • To investigate the impact of counterions on protein folding conformation when bound to nanoparticles.
  • To elucidate the mechanisms by which counterions influence protein stability.

Main Methods:

  • Protein folding energy calculations incorporating short-range (van der Waals, hydrogen bonds) and long-range (Coulomb) interactions.
  • Modeling counterion diffusion into bound proteins via charge-dipole and charge-induced dipole interactions.
  • Considering counterion solvation effects in the dispersing medium (e.g., water).

Main Results:

  • Counterion diffusion into bound proteins leads to partial unfolding, consistent with circular dichroism experiments.
  • The folding energy of bound proteins decreases with increasing counterion diffusion and polarizability.
  • Charge-dipole and charge-induced dipole interactions mediate the effect of counterions on protein residues.

Conclusions:

  • Counterions play a significant role in modulating the conformational stability of proteins adsorbed onto charged nanoparticles.
  • The findings provide insights into the behavior of protein-nanoparticle complexes and inform the design of such systems.