Which method can be used to evaluate enzymatic reactions in protein interactions?

In the context of evaluating enzymatic reactions in protein interactions, transport assays are specifically designed to assess the function of proteins, particularly membrane proteins and transporters. These assays typically measure the ability of a protein to transport substrates across membranes and can reveal information about enzymatic activity by monitoring how efficiently a substrate is moved or modified in the presence of specific enzymes.

Transport assays are beneficial for understanding how enzymes interact with substrates, providing insights into kinetic parameters and the regulatory factors affecting those interactions. They allow researchers to observe the direct impact of the enzyme's activity and its effect on substrates rather than simply identifying the presence of the proteins involved.

Other methods listed have different applications. Co-immunoprecipitation is primarily used to study protein-protein interactions by pulling down specific proteins from a mixture, whereas mass spectrometry focuses on identifying and measuring the mass of biomolecules, providing information about proteins and their modifications but not directly assessing enzymatic activity. Western blotting is another technique used to detect and analyze specific proteins in a sample, usually concentrated more on quantifying the presence of proteins rather than the functional dynamics of enzymatic reactions.