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Related Concept Videos

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Updated: Feb 23, 2026

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Terahertz absorption of lysozyme in solution.

Daniel R Martin1, Dmitry V Matyushov2

  • 1Department of Physics, Arizona State University, P.O. Box 871504, Tempe, Arizona 85287, USA.

The Journal of Chemical Physics
|September 3, 2017
PubMed
Summary

Radiation absorption in ideal protein solutions is primarily due to interfacial polarization, not solute dipole dynamics. Standard electrostatics fail, with a "Lorentz void" model better explaining experimental data for lysozyme solutions.

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Area of Science:

  • Physical Chemistry
  • Dielectric Theory
  • Biophysics

Background:

  • Radiation absorption by solutions is governed by frequency-dependent dielectric functions, a key aspect of dielectric theory.
  • For ideal solutions, dielectric theory separates polar response into void polarization and solute dipole response.
  • In protein solutions, terahertz frequency dynamics show minimal protein dipole moment fluctuations, suggesting a 'dynamically frozen' state.

Purpose of the Study:

  • To investigate the interfacial polarization contributing to radiation absorption in ideal protein solutions.
  • To compare theoretical models with experimental data for lysozyme solutions in the terahertz frequency domain.
  • To develop an analytical theory for solution absorption based on solute volume fraction.

Main Methods:

  • Application of analytical theory to model radiation absorption in ideal lysozyme solutions.
  • Utilizing computer simulations, including molecular dynamics, to calculate the cavity field response function.
  • Comparison of theoretical predictions with experimental measurements of solution absorption.

Main Results:

  • Maxwell electrostatics inaccurately describe protein-water interface polarization.
  • The 'Lorentz void' model provides a better fit to experimental data by not assuming interface polarization by external fields.
  • Analytical theory for absorption slope correlates well with molecular dynamics simulations and experimental results.

Conclusions:

  • Interfacial polarization, not protein dipole dynamics, dominates terahertz radiation absorption in ideal protein solutions.
  • The 'Lorentz void' model offers a more accurate framework than standard Maxwell electrostatics for this phenomenon.
  • The protein hydration shell acts as a distinct sub-ensemble not captured by conventional dielectric electrostatics.