DsRED oligomerization

Baird, G. S., Zacharias, D. A., and Tsien, R. Y. (2000). Biochemistry, mutagenesis, and oligomerism of DsRed, a red fluorescent protein from coral. Proc. Natl. Acad. Sci. USA 97 11984-11989. 

Lauf, U., Lopez, P. and Falk, M. M. (2001). Expression of fluorescently tagged connexins A novel approach to rescue function of oligomeric DsRed-tagged proteins. FEBS Lett. 498, 11-5. 

Fig. 2 Sdiematk of folding, chromophore formation, and chromophore modification of DsRed. The p-can structure represents the native conformation of the protein, while the denatured form is shown as an irregular chain. It is not known at which step oligomerization occurs, n-con-jugation for visible-light absorption is indicated in gray. Reprinted with permission from Miyawaki et al., Curr. Opin. Chem. Biol. 7,560 (2003). Copyright 2003 Elsevier...

Whether transfer of the dye pair GFP/DsRed or any analogous combinations to in vivo applications will work successfully depends on intracellular photon yields per molecule and the extent of fluorophore oligomerization. Nearly equal molecular brightness values for in vivo and in vitro situations were reported for EGFP implying that molecular brightness issues are unlikely to impede intracellular applications of the presented DsRed/GFP pair. Tetramerization of a reporter construct like STEV-ST devoid of any physiological role probably won t... 

---