2008Zhongguo shengwu huaxue yu fenzi shengwu xuebaoRequires access

Bimolecular Fluorescence Complementation Technique

Fan Jin

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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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What this paper is about

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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Available 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.

Key concepts: Bimolecular fluorescence complementation, Förster resonance energy transfer, Fluorescence, Protein–protein interaction, Green fluorescent protein, Biophysics, Complementation, Yellow fluorescent protein

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