Abstract
mCardinal2 is a red fluorescent protein developed through the designs of mKate, mNeptune and mCardinal. Fluorescence spectrums of mCardinal2 and its five mutants (T143C, T143G, C158A, C158D and M160E) were measured with their quantum yields. C158A and C158D increased brightness with slight changes in fluorescence spectrums while T143C, T143G and M160E decreased brightness with blue shift in fluorescence spectrums, which resulted in green, cyan and green fluorescent proteins respectively. Crystal structures of all six variants were analyzed and compared together with those of mKate, LSS-mKate1, LSS-mKate2 and mCardinal. Around the Cα-Cβ bond of Tyr64 in the MYG chromophores, only C158A and C158D were in the trans conformation while all others were mostly in the cis conformation. Blue-shift brightness-decreased variants (T143C, T143G and M160E) showed the diminished hydrogen bonds while large-Stoke-shift brightness-increased variant C158D showed the enhanced hydrogen bonds around the chromophore.
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