Nature Methods
- 3, 165 - 174 (2006)
Published online: 17 February 2006; | doi:10.1038/nmeth841
Illuminating insights into protein-protein interactions using bioluminescence resonance energy transfer (BRET)
Kevin D G Pfleger & Karin A Eidne
7TM Laboratory/Laboratory for Molecular Endocrinology, Western Australian Institute for Medical Research (WAIMR) and UWA Centre for Medical Research, University of Western Australia, Nedlands, Perth, Western Australia 6009, Australia.
Bioluminescence resonance energy transfer (BRET) is a straightforward biophysical technique for studying protein-protein interactions. It requires: (1) that proteins of interest and suitable controls be labeled with either a donor or acceptor molecule, (2) placement of these labeled proteins in the desired environment for assessing their potential interaction, and (3) use of suitable detection instrumentation to monitor resultant energy transfer. There are now several possible applications, combinations of donor and acceptor molecules, potential assay environments and detection system perturbations. Therefore, this review aims to demystify and clarify the important aspects of the BRET methodology that should be considered when using this technique.
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