Journal
BIOPOLYMERS
Volume 67, Issue 4-5, Pages 319-322Publisher
WILEY
DOI: 10.1002/bip.10115
Keywords
IR reflection absorption spectroscopy; circular dichroism; beta-lactoglobulin; air-water interface; protein folding
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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 (similar to40%, 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. (C) 2002 Wiley Periodicals, Inc.
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