Journal
ANALYTICAL BIOCHEMISTRY
Volume 498, Issue -, Pages 78-94Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ab.2015.11.021
Keywords
Protein aggregation; Turbidity; Mixed aggregation; Light scattering
Funding
- Australian National University Senior Research Fellowship
- Chinese government
- Australian National University
- Australian Research Council
- Nihon University
- Japanese Ministry of Education, Culture, Sports, Science, and Technology
- National Health and Medical Research Council of Australia
- Osaka University
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Due to their colloidal nature, all protein aggregates scatter light in the visible wavelength region when formed in aqueous solution. This phenomenon makes solution turbidity, a quantity proportional to the relative loss in forward intensity of scattered light, a convenient method for monitoring protein aggregation in biochemical assays. Although turbidity is often taken to be a linear descriptor of the progress of aggregation reactions, this assumption is usually made without performing the necessary checks to provide it with a firm underlying basis. In this article, we outline utilitarian methods for simulating the turbidity generated by homogeneous and mixed-protein aggregation reactions containing fibrous, amorphous, and crystalline structures. The approach is based on a combination of Rayleigh-Gans-Debye theory and approximate forms of the Mie scattering equations. Crown Copyright (C) 2015 Published by Elsevier Inc. All rights reserved.
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