mCherry

[2] mCherry belongs to the group of fluorescent protein chromophores used as instruments to visualize genes and analyze their functions in experiments.

Genome editing has been improved greatly through the precise insertion of these fluorescent protein tags into the genetic material of many diverse organisms.

mRFPs—like mCherry—are useful because they have a lower molecular weight and fold faster than tetramers, which results in reduced disturbance of the target system.

DsRed has low photostability (resistance to change under the influence of light) and a slow maturation rate (time until half the protein is folded).

mCherry, out of all of the true monomers developed, has the longest wavelengths, highest photostability, fastest maturation, excellent pH resistance, and is closest to mRFP1 in its excitation and emission maxima.

The chromophore in mCherry is made up of three amino acids, methionine, tyrosine, and glycine, which are post-translationally modified into an imidazolinone.

[12] It can be used to label bacteria to visualize them without antibiotic pressure[13] and also be used as a long-wavelength hetero-FRET (fluorescence resonant energy transfer) acceptor and probe for homo-FRET experiments.

Spectroscopic and atomic resolution crystallographic analyses of three representatives, mOrange, mStrawberry, and mCherry, reveal that different mechanisms operate to establish the excitation and emission maxima.

The electron-density map indicates the formation of a third heterocycle, 2-hydroxy-dihydrooxazole, upon the reaction of Thr 66 Oγ with the polypeptide backbone, which in turn reduces the conjugation of the carbonyl at position 65 with the rest of the chromophore.

In mStrawberry and mCherry, the movement of charged Lys 70 and protonation of Glu 215 are proposed to modify the chromophore electron-density distribution, inducing their signature red shift.