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A small-angle scattering study on equilibrium clusters in lysozyme solutions.

Anna Stradner¹, Frédéric Cardinaux, Peter Schurtenberger

¹Department of Physics, University of Fribourg, Chemin du Musée 3, CH-1700 Fribourg, Switzerland. anna.stradner@unifr.ch

The Journal of Physical Chemistry. B

|October 20, 2006

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Equilibrium clusters in lysozyme solutions are formed by short-range attraction and long-range repulsion. Cluster size increases with protein concentration and decreases with temperature.

Area of Science:

Biophysics
Soft Matter Physics
Protein Science

Background:

Recent studies suggest equilibrium clusters in protein solutions.
A low angle scattering contribution has been observed in various protein solutions.

Purpose of the Study:

Investigate structural properties of aqueous lysozyme solutions.
Examine conditions for equilibrium cluster formation.
Analyze factors influencing cluster structure.

Main Methods:

Small-angle scattering experiments.
Analysis using an equilibrium cluster model.

Main Results:

Lysozyme solutions exhibit cluster-cluster (q(c)) and monomer-monomer (q(m)) peaks.

Related Experiment Videos

Cluster formation is driven by attraction and repulsion forces.

Average cluster aggregation number (N(c)) increases with volume fraction, decreases with temperature, and increases with charge screening.

Conclusions:

Rising low q intensities are not universally indicative of long-range attraction in lysozyme.
Equilibrium clusters are crucial for self-assembly processes.
The simple globular cluster model provides quantitative analysis but has limitations.