Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 32, Issue 9, Pages 407-414Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2007.08.003
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Funding
- NIDDK NIH HHS [DK53434] Funding Source: Medline
- NIGMS NIH HHS [GM72048] Funding Source: Medline
- NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [R01DK053434] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [P20GM072048] Funding Source: NIH RePORTER
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Dynamic protein interactions play a significant part in many cellular processes. A technique that shows considerable promise in elucidating such interactions is Forster resonance energy transfer (FRET). When combined with multiple, colored fluorescent proteins, FRET permits high spatial resolution assays of protein-protein interactions in living cells. Because FRET signals are usually small, however, their measurement requires careful interpretation and several control experiments. Nevertheless, the use of FRET in cell biological experiments has exploded over the past few years. Here we describe the physical basis of FRET and the fluorescent proteins appropriate for these experiments. We also review the approaches that can be used to measure FRET, with particular emphasis on the potential artifacts associated with each approach.
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