Journal
BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 34, Issue -, Pages 679-682Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BST0340679
Keywords
fluorescence lifetime imaging microscopy (FLIM); fluorescent protein; Forster resonance energy transfer (FRET); living cell; protein-protein interaction; time-correlated single-photon counting (TCSPC)
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Funding
- Wellcome Trust [074146] Funding Source: Medline
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Recent developments in cellular imaging spectroscopy now permit the minimally invasive study of protein dynamics inside living cells. These advances are of interest to cell biologists, as proteins rarely act in isolation, but rather in concert with others in forming cellular machinery. Until recently, all protein interactions had to be determined in vitro using biochemical approaches: this biochemical legacy has provided cell biologists with the basis to test defined protein-protein interactions not only inside cells, but now also with high spatial resolution. These techniques can detect and quantify protein behaviours down to the single-molecule level, all inside living cells. More recent developments in TCSPC (time-correlated single-photon counting) imaging are now also driving towards being able to determine protein interaction rates with similar spatial resolution, and together, these experimental advances allow investigators to perform biochemical experiments inside living cells.
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