Bimolecular fluorescence complementation
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Bimolecular fluorescence complementation (BiFC) is a method of viewing the association of proteins inside living cells. Kerppola et al. (2002) solidified this methodology as viable in vivo.
[edit] How it works
The intact GFP protein (and its varient YFP, BFP, RFP ext) is flourecent, however when the GFP is split expressing both fragments does not restore flourecsence. Fusing of each of the two non-fluorescent fragments to two interacting partners leads to restioration of flourecense. This fluorescence is detected and recorded via a camera mounted on a fluorescence microscope. The advantage of the BiFC method over other methods of visualizing protein-protein interactions is that it gives on the one hand an indication of interaction and on the other allows to visulise the cellular localization of the complex.
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