| Abstract: | Background The green fluorescent protein (GFP) has been widely used in cell biology as a marker of gene expression, label of cellular
structures, fusion tag or as a crucial constituent of genetically encoded biosensors. Mutagenesis of the wildtype gene has
yielded a number of improved variants such as EGFP or colour variants suitable for fluorescence resonance energy transfer
(FRET). However, folding of some of these mutants is still a problem when targeted to certain organelles or fused to other
proteins. |
