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 -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 (40␟olume fraction). The layer thickness and the conformational properties of the protein do not depend on the bulk concentration. After adsorption of -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
Original language | English |
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Pages (from-to) | 319-322 |
Journal | Biopolymers |
Volume | 67 |
Issue number | 4-5 |
DOIs | |
Publication status | Published - 2002 |
Keywords
- β-lactoglobulin
- Air-water interface
- Circular dichroism
- IR reflection absorption spectroscopy
- Protein folding