Monomeric red-fluorescent protein

Campbell RE, Tour O, Palmer AE, Steinbach PA, Baird GS, Zacharias DA, Tsien RY (2002) A monomeric red fluorescent protein. Proc Natl Acad Sci USA 99 7877-7882... 

Verkhusha, V. V. and Sorkin, A. (2005). Conversion of the monomeric red fluorescent protein into a photoactivatable probe. Chem. Biol. 12,... 

G., and MiiUer-Taubenberger, A. (2004) A brilliant monomeric red fluorescent protein to visualize cytoskeleton dynamics in Dictyostelium. FEBS Lett. 577, 227-232... 

Mutants of monomeric red fluorescent protein mRFPl at residue 66 structure modeling by molecular dynamics and search for correlations with spectral properties. Biochemistry, Vol. 73, No. 10, pp. 1082-1095, ISSN 0006-2979 Kredel, S. Nienhaus, K Oswald, F. Wolff, M. Ivanchenko, S. Cymer, F. Jeromin, A. Michel, F. J. Spindler, K.D. Heilker, R. Nienhaus, G.U Wiedenmann, J. (2008). Optimized and far-red-emitting variants of fluorescent protein eqFP611. Chem. Biol, Vol. 15, pp. 224-233, ISSN 1074-5521... 

Shaner NC, Campbell RE, Steinbach PA, Giepmans BN, Palmer AE, Tsien RY (2004) Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nat Biotechnol 22 1567-1572... 

Stiel AC, Andresen M, Bock H et al (2008) Generation of monomeric reversibly switchable red fluorescent proteins for far-field fluorescence nanoscopy. Biophys J 95 2989-2997... 

Engineering of a monomeric green-to-red photoactivatable fluorescent protein induced by blue light. Nat. Biotechnol. 24, 461-5. 

Receptors can be labeled genetically by fusion with fluorescent proteins. Doing so ensures that each protein of interest is labeled with exactly one fluorescent tag, an important feature for quantitative single-molecule studies. Both GFP and YFP can be used for single-molecule imaging. All red variants of these proteins are either not monomeric or not photostable enough for serious single-molecule analysis. 

In this chapter, a new approach based on the simultaneous use of nonlinear laser fluorimetry, spectrophotometry and conventional fluoiimetiy methods is presented. The approach allows us to in vroo determine the individual photophysical parameters of fluorophores in multi-fluorophore protein complexes. The ap>proach has been applied for investigation of the photophysical properties of the protein molecules of different complexity. Two classes of proteins have been chosen, namely, serum albumins (by the examples of human and bovine serum albumins) and fluorescent proteins (by the example of monomeric red FP mRFPl). The following new results are ptresented. 

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