Bimolecular Fluorescence Complementation Technique
Fan Jin
Abstract
Fan Jin
Abstract
Biomolecular fluorescence complementation (BiFC) is a recently developed new technique to detect the protein-protein interactions in vitro and in vivo. The technique is based on the principle that two nonfluorescent fragments of a fluorescent protein dissected at appropriate site are brought together and reconstructed to fluorescence, depending on the association or interaction between the proteins fused to each fragment. BiFC method not only enables directly visualization and localization of protein interactions but also is simple and noninvasive. Moreover, multiple color BiFC systems or combing BiFC and fluorescence resonance energy transfer (FRET) technology may be exploited to detect the multiple protein-protein interactions.
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Biomolecular fluorescence complementation (BiFC) is a recently developed new technique to detect the protein-protein interactions in vitro and in vivo. The technique is based on the principle that two nonfluorescent fragments of a fluorescent protein dissected at appropriate site are brought together and reconstructed to fluorescence, depending on the association or interaction between the proteins fused to each fragment. BiFC method not only enables directly visualization and localization of protein interactions but also is simple and noninvasive. Moreover, multiple color BiFC systems or combing BiFC and fluorescence resonance energy transfer (FRET) technology may be exploited to detect the multiple protein-protein interactions.
Key concepts: Bimolecular fluorescence complementation, Förster resonance energy transfer, Fluorescence, Protein–protein interaction, Green fluorescent protein, Biophysics, Complementation, Yellow fluorescent protein