Expression-Enhanced Fluorescent Proteins Based on Enhanced Green Fluorescent Protein for Super-resolution Microscopy

We present the development of robustly photoswitchable variants of enhanced green fluorescent protein (EGFP), named rsGreens, that display up to 30-fold higher fluorescence in E. coli colonies grown at 37 °C and more than 4-fold higher fluorescence when expressed in HEK293T cells compared to their ancestor protein rsEGFP.
Duwé S et al., ACS Nano, 2015, 9 (10), pp 9528–9541
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The first ever crystal structures of a negative reversibly switchable fluorescent protein derived from Aequorea victoria - called rsGreen0.7 -was determined in both the “on”- and “off”-conformation and provided further insights into the mechanisms underlying the photochromism. During photoswitching several structural rearrangements such as a cis-trans isomerization, backbone shifts and changes in hydrogen bonding occur.
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Expression-Enhanced Fluorescent Proteins Based on Enhanced Green Fluorescent Protein for Super-resolution Microscopy;
Duwé S., De Zitter E., Gielen V., Moeyaert B., Vandenberg W., Grotjohann T., Clays K.,
Jakobs S., Van Meervelt L., and Dedecker P.,
ACS NANO, 2015, 9 (10), pp 9528–9541 10.1021/acsnano.5b04129
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