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Comment
. 2013 Oct 24;20(10):1203-5.
doi: 10.1016/j.chembiol.2013.10.004.

Bridging the spectral gap in fluorescent proteins through directed evolution

Paul B Whittredge  1 , Justin W Taraska
Affiliations
Comment

Bridging the spectral gap in fluorescent proteins through directed evolution

Paul B Whittredge et al. Chem Biol. .

Abstract

Fluorescent proteins are used as noninvasive tags for protein trafficking, structure, and action. In this issue of Chemistry & Biology, Hoi and colleagues present a new optimized zFP538 yellow fluorescent protein called mPapaya1 that is bright, monomeric, and an excellent fusion partner for cellular proteins.

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Figures

Figure 1
Figure 1
Yellow fluorescent protein from Zoanthus sp. A) The Zoanthus button polyp. B) The crystal structure of the yellow fluorescent protein zFP538 and its chromophore (C). D) The emission spectrum of the mPapaya1 protein (white line). The emission peak is at 541 nm. Photo of Zoanthus sp. courtesy of Coral Morphologic.
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References

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