Final answer:
Enzyme inhibition constants for multi-inhibitors can be assayed using UV spectroscopy, circular dichroism, fluorescence spectroscopy, and docking studies.
Step-by-step explanation:
Enzyme inhibition constants for multi-inhibitors can be assayed using various methods. One commonly used method is UV spectroscopy, which measures the absorbance of light by the enzyme-inhibitor complex. The inhibition constants can then be calculated using the initial velocity data and a Lineweaver-Burk plot. Another method is circular dichroism, which measures changes in the enzyme's secondary structure upon interaction with inhibitors. Additionally, fluorescence spectroscopy and docking studies can provide information about enzyme-inhibitor interactions and binding sites.