Limited conformational change of beta-lactoglobulin when adsorbed at the air-water interface

M.B.J. Meinders, H.H.J. de Jongh

    Research output: Contribution to journalArticleAcademicpeer-review

    30 Citations (Scopus)

    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 languageEnglish
    Pages (from-to)319-322
    JournalBiopolymers
    Volume67
    Issue number4-5
    DOIs
    Publication statusPublished - 2002

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