Fluorescence microscopy provides a non-invasive means for visualising dynamic protein interactions. As well as allowing the calculation of kinetic processes via the use of time-resolved fluorescence, localisation of the protein within cells or model systems can be monitored. These fluorescence lifetime images (FLIM) have become the preferred technique for elucidating protein dynamics due to the fact that the fluorescence lifetime is an absolute measure, in the main independent of fluorophore concentration and intensity fluctuations caused by factors such as photobleaching. In this work we demonstrate the use of a time-resolved fluorescence microscopy, employing a high repetition rate laser excitation source applied to study the influence of a metal surface on fluorescence tagged protein and to elucidate viscosity using the fluorescence lifetime probe DASPMI.
|Title of host publication||Proceedings of SPIE Volume 7903: Multiphoton Microscopy in the Biomedical Sciences XI|
|Editors||A. Periasamy, K. König, P.T.C. So|
|Number of pages||11|
|Publication status||Published - 2011|
- fluorescence microscopy
- tagged protein
- protein interactions