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

article
2003
Kudryashova, E.V.

Meinders, M.B.J.

Visser, A.J.W.G.

Hoek, A. van

Jongh, H.H.J. de
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 β-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.
Topics
Food technologyInfrared reflection absorption spectroscopyProtein structureSurface compressionSurface layerTime-resolved fluorescence anisotropyEgg whiteOvalbuminProteinWaterAbsorption spectroscopyAdsorptionAirAnisotropyBeta sheetCompressionDynamicsFluorescenceNonhumanPressureProtein aggregationProtein foldingProtein protein interactionProtein structureAdsorptionAirColloidsEgg ProteinsOligopeptidesOvalbuminProtein ConformationProtein Structure, SecondarySpectrometry, FluorescenceSpectrophotometry, InfraredStructure-Activity RelationshipSurface PropertiesSurface TensionWater
TNO Identifier
237238
Repository link
https://resolver.tno.nl/uuid:425367e3-c4df-4f1d-99da-8eaf43e273e6
ISSN
01757571
Source
European Biophysics Journal, 32(6), pp. 553-562.
Pages
553-562
Files
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