Structure and dynamics of egg white ovalbumin adsorbed at the air/water interface

E.V. Kudryashova, M.B.J. Meinders, A.J.W.G. Visser, A. van Hoek, H.H.J. de Jongh

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48 Citations (Scopus)


The molecular properties of egg white ovalbumin adsorbed at the air/water interface were studied using infrared reflection absorption spectroscopy (IRRAS) and time-resolved fluorescence anisotropy (TRFA) techniques. Ovalbumin adsorbed at the air/water interface adopts a characteristic partially unfolded conformation in which the content of the beta-sheet is 10% lower compared to that of the protein in bulk solution. Adsorption to the interface leads to considerable changes in the rotational dynamics of ovalbumin. The results indicate that the end-over-end mobility of the ellipsoidal protein becomes substantially restricted. This is likely to reflect a preferential orientation of the protein at the interface. Continuous compression of surface layers of ovalbumin causes local aggregation of the protein, resulting in protein-network formation at the interface. The altered protein-protein interactions contribute to the strong increase in surface pressure observed.
Original languageEnglish
Pages (from-to)553-562
Number of pages10
JournalEuropean Biophysics Journal
Publication statusPublished - 2003


  • air-water-interface
  • time-resolved fluorescence
  • beta-casein
  • neutron reflectivity
  • infrared-spectroscopy
  • adsorption properties
  • circular-dichroism
  • liquid interfaces
  • surface-tension
  • proteins


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