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Updated: Jan 22, 2026

Passaging Human Neural Stem Cells
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Passage through a sub-diffusing geometrical bottleneck.

K L Sebastian1

  • 1Indian Institute of Technology, Palakkad, Ahalia Integrated Campus, Kozhippara P.O., Palakkad 678557, India.

The Journal of Chemical Physics
|July 15, 2019
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Summary
This summary is machine-generated.

Protein ligand binding rates depend on medium viscosity. A new subdiffusion model explains experimental observations where rates show a viscosity dependence (η-ν) not predicted by traditional theories, aligning with protein dynamics.

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Area of Science:

  • Chemical Physics
  • Biophysics
  • Physical Chemistry

Background:

  • Kramers theory predicts reaction rates inversely proportional to medium viscosity (η).
  • Experimental ligand-protein binding shows rates proportional to η-ν (ν=0.4-0.8).
  • Zwanzig's fluctuating gate model predicts η-1/2 dependence, partially explaining observations.

Purpose of the Study:

  • To generalize Zwanzig's model by incorporating subdiffusion of the opening.
  • To explain the observed viscosity dependence of ligand-protein binding rates.
  • To reconcile theoretical predictions with experimental findings in condensed media.

Main Methods:

  • Developing a generalized Zwanzig model where the opening size undergoes subdiffusion.
  • Solving the model to derive the rate dependence on viscosity.
  • Comparing theoretical predictions with experimental data.

Main Results:

  • The generalized model predicts reaction rates proportional to η-ν, with ν ranging from 0.5 to 1.
  • This viscosity dependence aligns with experimental observations of ligand-protein binding.
  • Subdiffusion of the opening is key to explaining the observed rate behavior.

Conclusions:

  • Subdiffusion in protein dynamics is crucial for understanding ligand binding rates.
  • The generalized Zwanzig model provides a theoretical framework for observed viscosity dependencies.
  • This work bridges the gap between Kramers theory and experimental ligand-protein binding kinetics.