How Can Non-Competitive Inhibition be Identified Experimentally?
Non-competitive inhibition can be identified through various experimental techniques. One common method is to perform enzyme kinetics assays by measuring the reaction rate at different substrate and inhibitor concentrations. A hallmark of non-competitive inhibition is that the Lineweaver-Burk plot (a double reciprocal plot of 1/[S] vs. 1/V) will show lines that intersect on the x-axis, indicating a change in Vmax but no change in Km. Additionally, spectroscopic techniques and X-ray crystallography can be used to visualize the binding of inhibitors to allosteric sites on enzymes.
