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Updated: Apr 22, 2026

Single-Molecule Tracking Microscopy - A Tool for Determining the Diffusive States of Cytosolic Molecules
Published on: September 5, 2019
Concentration dependence of translational diffusion coefficients for globular proteins
David J Scott1, Stephen E Harding, Donald J Winzor
1National Centre for Macromolecular Hydrodynamics, School of Biosciences, University of Nottingham, Sutton Bonington, LE 12 5RD, UK. david.scott@nottingham.ac.ak.
This study on protein diffusion found that the translational diffusion coefficient is largely concentration-independent at low protein concentrations, supporting approximations used in sedimentation velocity analysis.
Area of Science:
- Biophysical Chemistry
- Protein Dynamics
- Solution Behavior
Background:
- Sedimentation velocity experiments analyze protein diffusion.
- The translational diffusion coefficient (D) is often assumed to be concentration-independent.
- Current theories predict significant concentration dependence of D for proteins.
Purpose of the Study:
- To evaluate the concentration independence assumption for D in protein analysis.
- To assess the applicability of Fujita's Lamm equation approximation.
- To investigate diffusion of ovalbumin and bovine serum albumin.
Main Methods:
- Analysis of published traditional diffusion experiments.
- Examination of protein diffusion under constant temperature and solvent chemical potential.
- Comparison of experimental data with theoretical predictions.
Main Results:
- No significant concentration dependence of D was detected for ovalbumin and bovine serum albumin.
- Observed minor concentration dependence aligns with solution viscosity effects.
- Predicted variation in D below 10 mg mL(-1) falls within experimental uncertainty.
Conclusions:
- The assumption of concentration independence for D is reasonable for proteins at low concentrations.
- Fujita's approximate solution of the Lamm equation is suitable for analyzing boundary spreading in sedimentation velocity experiments.
- Findings support the use of simplified models in protein biophysical characterization.
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