Structure and dynamics of egg white ovalbumin adsorbed at the air/water interface.
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.
Kudryashova
Elena V
EV
Division of Chemical Enzymology, Chemistry Department, Moscow State University, 119899 Moscow, Russia.
Meinders
Marcel B J
MB
Visser
Antonie J W G
AJ
van Hoek
Arie
A
de Jongh
Harmen H J
HH
D000327:Adsorption; D000388:Air; D003102:Colloids / Q000737:chemistry*; D004527:Egg Proteins / Q000737:chemistry / Q000648:ultrastructure; D009842:Oligopeptides; D010047:Ovalbumin / Q000737:chemistry* / Q000648:ultrastructure*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D013050:Spectrometry, Fluorescence / Q000379:methods*; D013055:Spectrophotometry, Infrared / Q000379:methods*; D013329:Structure-Activity Relationship; D013499:Surface Properties; D013500:Surface Tension; D014867:Water / Q000737:chemistry*
D003102:Colloids; D004527:Egg Proteins; D009842:Oligopeptides; D014867:Water; C048812:kinetensin; D010047:Ovalbumin