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Dual-polarization interferometry
Dual-polarization interferometry (DPI) is an analytical technique that probes molecular layers adsorbed to the surface of a waveguide using the evanescent wave of a laser beam. It is used to measure the conformational change in proteins, or other biomolecules, as they function (referred to as the conformation activity relationship).
==Instrumentation==
DPI〔 〕 focuses laser light into two waveguides. One of these functions as the "sensing" waveguide having an exposed surface while the second one functions to maintain a reference beam. A two-dimensional interference pattern is formed in the far field by combining the light passing through the two waveguides. The DPI technique rotates the polarization of the laser, to alternately excite two polarization modes of the waveguides. Measurement of the interferogram for both polarizations allows both the refractive index and the thickness of the adsorbed layer to be calculated. The polarization can be switched rapidly, allowing real-time measurements of chemical reactions taking place on a chip surface in a flow-through system. These measurements can be used to infer conformational information about the molecular interactions taking place, as the molecule size (from the layer thickness) and the fold density (from the RI) change. DPI is typically used to characterize biochemical interactions by quantifying any conformational change at the same time as measuring reaction rates, affinities and thermodynamics.
The technique is quantitative and real-time (10 Hz) with a dimensional resolution of 0.01 nm.〔 〕
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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