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Characterization of Proteins by Size-Exclusion Chromatography Coupled to Multi-Angle Light Scattering (SEC-MALS)
Published on: June 20, 2019
Lysozyme aggregation studied by light scattering. II. Variations of protein concentration
Y Georgalis1, P Umbach, J Raptis
1Institut für Kristallographie, Freie Universität Berlin, Germany. yannis@chemie.fu-berlin.de
Acta Crystallographica. Section D, Biological Crystallography
|August 10, 2004
Summary
This study observed lysozyme aggregation using light scattering, revealing fractal structures and changes around 2.0 mM. These findings help predict crystallization behavior in protein solutions.
Area of Science:
- Biophysics
- Materials Science
- Protein Crystallization
Background:
- Lysozyme aggregation is crucial for understanding protein crystallization.
- Controlling protein-protein interactions is key to managing aggregation pathways.
Purpose of the Study:
- To investigate the aggregation behavior of nucleating lysozyme solutions.
- To correlate aggregation dynamics with crystallization propensity.
Main Methods:
- Utilized static and dynamic light scattering techniques.
- Examined lysozyme solutions across concentrations (0.34–3.08 mM).
- Employed NaCl and (NH4)2SO4 to modulate Coulombic interactions and induce aggregation.
Main Results:
- Observed coexistence of mass-fractals and smaller lysozyme oligomers.
- Fractal growth kinetics showed distinct concentration-dependent tendencies, changing significantly around 2.0 mM.
- Static light scattering indicated restructuring into compact structures during later aggregation stages.
Conclusions:
- The study provides insights into lysozyme aggregation pathways.
- Correlations between observables suggest a method for predicting protein crystallization.
- A tentative scheme for prominent structures in nucleating lysozyme solutions is proposed.
