Study conformational changes of transglutaminase when binding Ca2+ by Dual polarization interferometry (DPI) (CAT#: STEM-MB-0382-WXH)

Name: Study conformational changes of transglutaminase when binding Ca2+ by Dual polarization interferometry (DPI)
SKU: STEM-MB-0382-WXH
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Introduction

Transglutaminases are enzymes involved in the post-translational modification of proteins, forming isopeptide bonds at glutamine residues. The primary function of these enzymes appears to be in the stabilization of tissues and as such their occurrence is widespread, being found in both extracellular and cellular fluids.

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Principle Applications Procedure Materials

Principle

Dual polarization interferometry (DPI) is an analytical technique that allows the simultaneous determination of thickness, density, and mass of a biological layer on a sensing waveguide surface in real time. 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. 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.

Applications

Study the conformational changes of transglutaminase when binding Ca2+.
Drug discovery.

Procedure

1. Setting of dual polarization interferometry
2. Preparing the DPI sensor chip
3. Immobilization of target on DPI biosensor
4. Reagent was injected to react
5. Quantitative analysis