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  • Title: Limited conformational change of beta-lactoglobulin when adsorbed at the air-water interface.
    Author: Meinders MB, De Jongh HH.
    Journal: Biopolymers; 2002; 67(4-5):319-22. PubMed ID: 12012457.
    Abstract:
    Detailed insight can be obtained from proteins at and near the air-water interface using external reflection IR and circular dichroism techniques. Besides information on local protein concentrations and surface layer thickness, it is shown that beta-lactoglobulin displays a limited unfolding at the interface. The conformational change is comparable to that observed upon heat-induced aggregation of the protein and can be understood in view of the high surface concentration of the protein (approximately 40% volume fraction). The layer thickness and the conformational properties of the protein do not depend on the bulk concentration. After adsorption of beta-lactoglobulin to a preformed lipid monomolecular layer a similar conformational change is induced, suggesting that the folding properties of the protein itself determine the extent of conformational changes at the interfaces.
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