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Studying Changes in Protein Structure using Dual Polarization Interferometry

This talk will examine the use a surface characterization technique known as Dual Polarization Interferometry (DPI) for the physical analysis of changes in protein structure. The analysis is achieved by measuring the dimensions, refractive index (density) and mass of mono-layers of protein deposited on an optical waveguide surface in real time. Structural changes in the protein layer can be measured as a consequence of physical perturbations to the local environment such as pH, salt concentration and temperature in addition to changes resulting from directly from binding interactions. The measurement of streptavidin – biotin interactions using DPI will be discussed as a model system. Example applications will be presented which will include binding interactions such as protein – protein, protein – small molecule, protein – metal ion, protein – carbohydrate and protein – DNA.

Type:	Dual Polarization Interferometry (DPI)
Duration:	39 minutes
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