Premium
Limited conformational change of β‐lactoglobulin when adsorbed at the air–water interface
Author(s) -
Meinders Marcel B. J.,
De Jongh Harmen H. J.
Publication year - 2002
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.10115
Subject(s) - chemistry , conformational change , circular dichroism , adsorption , beta lactoglobulin , folding (dsp implementation) , crystallography , biophysics , protein folding , protein adsorption , chemical physics , whey protein , chromatography , stereochemistry , biochemistry , electrical engineering , biology , engineering
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 β‐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% volume fraction). The layer thickness and the conformational properties of the protein do not depend on the bulk concentration. After adsorption of β‐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. © 2002 Wiley Periodicals, Inc. Biopolymers (Biospectroscopy) 67: 319–322,2002