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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October 2006
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Conference Article|
October 25 2006
Fluorescence lifetime imaging microscopy (FLIM) to quantify protein–protein interactions inside cells
R.R. Duncan
R.R. Duncan
1
1Centre for Integrative Physiology, University of Edinburgh, Hugh Robson Building, George Square, Edinburgh EH8 9XD, Scotland, U.K.
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Publisher: Portland Press Ltd
Received:
August 01 2006
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2006 The Biochemical Society
2006
Biochem Soc Trans (2006) 34 (5): 679–682.
Article history
Received:
August 01 2006
Citation
R.R. Duncan; Fluorescence lifetime imaging microscopy (FLIM) to quantify protein–protein interactions inside cells. Biochem Soc Trans 1 October 2006; 34 (5): 679–682. doi: https://doi.org/10.1042/BST0340679
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