Comparisons To Other Technologies
Most techniques used to study protein–protein interactions rely on in vitro methods. Unfortunately, studying proteins in an artificial system, outside of their cellular environment, poses a number of difficulties. For example, this may require the removal of proteins from their normal cellular environment. The processing required to isolate the protein may affect its interactions with other proteins. In addition, isolating the protein from the intracellular signaling and mechanisms that occur in the normal cell may provide a misleading picture of intracellular and physiological occurrences. Furthermore, proteins studied in vitro may be studied at concentrations vastly different from their normal abundance levels, may not necessarily be transported efficiently into the cells, or may not be selective enough to function in the host genome. Finally, by studying proteins in vitro, one is unable to determine the influence of specific protein–protein interactions in the cell on the functional or physiological consequences.
Other in vivo assays most commonly used to study protein–protein interactions include fluorescence resonance energy transfer (FRET) and yeast two-hybrid (Y2H) assay. Each of these assays has their advantages and disadvantages in comparison to BiFC:
Read more about this topic: Bimolecular Fluorescence Complementation
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