ABSTRACT
Protein-protein interactions are known to play an important role in a variety of biochemical systems. To date, thousands of protein-protein interactions have been identified by using the conventional two-hybrid system, but this method is limited in that the interaction must occur in the yeast nucleus. This means interactions that strictly depend upon cell-type-specific processing or compartmentalization will not be detected. Therefore, a number of new methods have been developed recently that rely on reconstitution of biochemical function
in vivo
, such as fluorescence resonance energy transfer (FRET), protein mass spectrometry, or evanescent wave.
