Journal
CURRENT OPINION IN COLLOID & INTERFACE SCIENCE
Volume 8, Issue 6, Pages 515-522Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.cocis.2004.01.008
Keywords
colloids; protein solutions; light scattering
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The solution behaviour of globular proteins still presents many puzzling aspects, calling for a deeper understanding of the physical properties of lyophilic colloids. For instance, protein interactions in 'salting-out' conditions require to take explicitly into account 'Donnan' effects on the small ion distribution, while understanding of temperature and salt-specificity effects on protein solubility presumably calls for a careful analysis of hydrophobic contributions. Yet, very unexpected effects can be found even at low salt concentration. In particular, we discuss the very distinctive properties of beta-lactoglobulin A (BLGA) solutions, where strong attractive interactions show up, displaying a marked non-monotonic trend as a function of the solution ionic strength. These 'anomalous' attractions drive very peculiar reversible association processes, resulting in the spontaneous formation of short-lived clusters with a well-defined small aggregation number. We suggest that other protein association processes of physiological interest may parallel BLGA clustering. (C) 2004 Elsevier Ltd. All rights reserved.
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