
%0 Journal Article
%A Holt, S. A. 
%A Henderson, M. J. 
%A White, J. W. 
%T Thermal Denaturation of Interfacial Protein Layers
%J Australian Journal of Chemistry
%D 2002/09/19
%V 55
%N 7
%P 449-459
%K 
%R https://doi.org/10.1071/CH02100
%U https://www.publish.csiro.au/paper/CH02100 
%X We report for the first time the structural measurements at nanometre resolution of the denaturation of &#946;-lactoglobulin and lysozyme at an air&#8211;water interface using the technique of neutron reflectivity. The incipient denaturation shown previously[1] for myogloblin is also studied for these molecules at room temperature, and denaturation is provoked by increasing the temperature of the solutions progressively to 75&#176;C. The change in the adsorbed protein layer thickness, its scattering length density and density distribution perpendicular to the surface as a function of increased temperature are reported and the data analysed in terms of a two-state model for the denaturation process. These measurements are relevant to an understanding of the way in which proteins at interfaces act as templates, for example, in biomineralization. 
