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Fluorescent proteins DsRed

Habuchi S, Cotlet M, Gensch T, Bednarz T, Haber-Pohlmeier S, Rozenski J, Dirix G, Michiels J, Vanderleyden J, Heberle J, De Schryver FC, Hofkens J (2005) Evidence for the isomerization and decarboxylation in the photoconversion of the red fluorescent protein DsRed. J Am Chem Soc 127 8977-8984... [Pg.380]

Similarly to dyes, some fluorescent proteins can be incorporated into polymeric beads to be used as an alternative for ion sensing. For example, a reporter protein (composed of a phosphate-binding protein, a FRET donor (cyan fluorescent protein) and a FRET acceptor (yellow fluorescent protein)) was incorporated into polyacrylamide nanobeads by Sun et al. [46]. FRET was inhibited upon binding of phosphate. Kopelman and co-workers [47] used a similar approach to design a nanosensor for copper ions. They have found that fluorescence of red fluorescent protein DsRed (commonly used as a label) is reversibly quenched by Cu2+ and Cu+. Both DsRed and Alexa Fluor 488 (used as a reference) were entrapped into polyacrylamide nanobeads. Typically, up to 2 ppb of copper ions can be reliably measured. It should be mentioned, that in contrast to much more robust dyes, mild conditions upon polymerization and purification are very important for immobilization of the biomolecule to avoid degradation. [Pg.211]

Recently, a photoactivatable variant from Aequoria victoria green fluorescent protein (pa-GFP) was reported (Patterson and Lippincott-Schwartz 2002), yielding an increase in fluorescence emission intensity (at k 520 nm) by a factor of 100 when excited at k 488 nm after spectral activation at A. 408 nm. This phenomenon is due to an internal photoconversion process in the protein and allows spectral photoactivation of this protein in a very local way such as in the nucleus of a living cell (Post et al. 2005). In tobacco BY-2 protoplasts, we transiently co-expressed pa-GFP or pa-GFP fusion proteins and red-fluorescent protein (DsRed)-tagged prenylated Rab acceptor 1 (Pral At2g38360), a membrane protein that localizes in speckles around the nuclear envelope. The DsRed transfection allows proper cell identification and visualization before activation (via Pral -DsRed fluorescence). After pa-GFP... [Pg.309]

Hsiao YW, Sanchez-Garcia E, Doerr M, Thiel W (2010) Quantum refinement of protein structures implementation and application to the red fluorescent protein DsRed.Ml. J Phys ChemB 114 15413-15423... [Pg.116]

Other naturally occurring fluorescent proteins have been found in aquatic organisms including reef corals and sea anemones. The red fluorescent protein DsRed was discovered in the Anthozoan genus Discosoma. The DsRed fluorescent protein fluorophore features an imidazoline ring system similar to the GFP fluorophore but... [Pg.701]

M. Cotlet, J. Hofkens, S. Habuchi, G. Dirix, M. Van Guyse, J. Michiels, J. Vanderleyden, F.C. De Sehryver, Identification of different emitting species in the red fluorescent protein DsRed by means of ensemble and single molecule spectroscopy, PNAS 98, 14398-5006 (2001)... [Pg.357]

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. [Pg.381]

Gross LA, Baird GS, Hoffman RC, Baldridge KK, Tsien RY (2000) The structure of the chromophore within DsRed, a red fluorescent protein from coral. Proc Natl Acad Sci USA 97 11990-11995... [Pg.374]

The second major breakthrough for the application of fluorescent proteins was the isolation of the red fluorescent protein (RFP) drFP583 or DsRed from the Anthozoa and Discosoma sp., a mushroom-shaped anemone found in the warm waters of the Indo-Pacific ocean [13], The breakthrough was not only the discovery of the first true RFP, but equally important was the fact that it was discovered in a nonbioluminescent species and that the gene was cloned immediately. [Pg.185]

Single-molecule photophysics of DsRed, a red fluorescent protein [119]... [Pg.42]

A.A. Heikal, S.T. Hess, G.S. Baird, R.Y. Tsien, W.W. Webb, Molecular spectroscopy and dynamics of intrinsically fluorescent proteins Coral red (dsRed) and yellow (Citrine). PNAS 97(22), 11996-12001 (2000)... [Pg.116]

Examples of fluorescence labels for hgands are carboxyfluorescein, Cy3, a commercially available fluorescent marker based on a cyanine dye or tetramethyl-rhodamine. They are chemically introduced into a ligand. As with the radioactive labels, a possible influence of the labels on the binding behavior of the labeled hgands has to be considered, especially as the fluorescent dyes are complex molecules. Furthermore, the receptors themselves can be fluorescent labeled, which is done recombinantly. The respective receptors are expressed as fusion proteins with fluorescent proteins, e.g., green fluorescent protein (GFP) from Aequorea victoria, one of its mutant variants, or DSRed from Discosoma striata [26, 35]. [Pg.116]

However, during the last decade a number of GFP mutants were described showing altered spectral properties and/or improved solubility upon expression in heterologous systems. In addition, numerous other naturally occurring fluorescent proteins were described such as the red-fluorescent protein from Discosoma sp. (DsRED). A comprehensive description of the available fluorescent proteins is given including the spectral properties, amino-acid sequence alignments, comparisons of the secondary and tertiary structures of the proteins. [Pg.3]

Due to its unique red-fluorescence the DsRED protein gained strong interest amongst researchers, but it soon turned out that the usability of this protein as a reporter is limited by several factors its... [Pg.6]

As already mentioned the red-fluorescent protein drFP583 is commercially available under the name DsRED. According to the... [Pg.54]

In our own work fluorescence of DsRED and its derivatives DsRED2, DsRED.T3 and DsRED.T4 proved to be stable even throughout prolonged fluorescence microscopy or measurements of spectral properties. Under similar conditions equaRFPl (eqFP611) bleached rapidly (Jach, unpublished observations), which is in contrast to pub-lished data indicating that this protein should as stable as DsRED [35]. [Pg.55]


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See also in sourсe #XX -- [ Pg.184 ]




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