Final answer:
Protein interactions can be detected using mass spectrometry, X-ray crystallography, NMR, protein microarrays, immunoprecipitation, enzyme immunoassays (EIAs), and western blots. These methods enable precise identification and structural characterization of the proteins.
Step-by-step explanation:
Other types of assays that detect protein interactions include mass spectrometry, which identifies and determines the characteristics of molecules; X-ray crystallography and nuclear magnetic resonance (NMR) for determining three-dimensional structures; protein microarrays for studying interactions; immunoprecipitation coupled with microarrays for protein binding site occupancy; and various types of enzyme immunoassays (EIAs), which use antibodies to visualize or quantify antigens. Additionally, western blots rely on antibodies to detect specific proteins after gel electrophoresis.
Enzyme immunoassays, for instance, can be conducted in microtiter plates and use antibody molecules with an attached enzyme that binds its specific antigen, revealing the presence of the antigen upon adding a substrate. In western blots, proteins are transferred to a membrane and identified with antibodies linked to enzymes or fluorophores. These techniques are crucial for clinical diagnostics and researching pathogen identification.