The movement of proteins in a temperature gradient is a sensitive and versatile way to probe protein interactions, including the important class of membrane receptors binding to its target molecule and fragment screens for pharmaceutical compounds. The binding can be detected ail-optically in various biological fluids, including in blood serum and cell lysate. While labelling adds specificity to the measurement process, label free detection of binding is possible. The physical basis of the movement was studied with DNA and polystyrene beads and could be understood with a capacitor model of ionic shielding. Recently, we were able to achieve thermophoretic movement inside living cells.
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