BIOT 505 Lecture Notes - Lecture 6: Equilibrium Constant, Total Internal Reflection Fluorescence Microscope, Fluorometer
2 Jan 2018
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Label-f(cid:396)ee a(cid:374)al(cid:455)sis of (cid:862)bio(cid:373)ole(cid:272)ules(cid:863) mark a. hancock (biochemist) Aim: how was they interact, how strong/weak are those interactions: protein interaction (networks) The study of biomolecules is critical for understanding health, disease, and drug design. 96-well plate, one of the proteins are immobilized: enzyme-linked immunosorbent assay (elisa): gives qualatative answer for binding interaction i. e a yes/no. is a great starting point. Can show if show if there is point of saturation: radioimmunosorbant assay (ria): data similar, but get measure of non-specific binding of protein to wells, and specific binding when subtract total binding non-specific. Can fit the data to a binding model to determine overall strength of association (kd value). In cuvette, water bath to maintain temperature, fluorimeter (more cost involved) Approach to fit data to binding model, to get kd value. All in solution, so protein is not immobilized (advantage)
