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Untersuchte Arbeit:
Seite: 14, Zeilen: 13-19
Quelle: Schaefer 2007b
Seite(n): 58, Zeilen: 22ff
However, with its low quantum yield (˂0.001), and comparatively slow switching kinetics, the photochromic properties of asFP595 are far from being optimal.

Recently, high-resolution crystal structures of wt asFP595 in its off state (Andresen et al., 2005; Willmann et al., 2005; Quillin et al., 2005), of the Ser158Val mutant in its on state, and of the Ala143Ser mutant in its on and off states (Andresen et al., 2005) were determined (fig 7).

Currently, however, with its low quantum yield (< 0.1% and 7% before and after activation, respectively [8, 203]) and rather slow switching kinetics, the photochromic properties of asFP595 need to be improved. [...]

High-resolution crystal structures of wild-type (wt) asFP595 in its off state [205, 206, 207], of the Ser158Val mutant in its on state, and of the Ala143Ser mutant in its on and off states [205] were recently determined.


[8] K. A. Lukyanov, A. F. Fradkov, N. G. Gurskaya, M. V. Matz, Y. A. Labas, A. P. Savitsky, M. L. Markelov, A. G. Zaraisky, X. N. Zhao, Y. Fang, W. Y. Tan and S. A. Lukyanov. Natural animal coloration can be determined by a nonfluorescent green fluorescent protein homolog. J. Biol. Chem., 275(34):25879–25882, 2000.

[203] K. A. Lukyanov, D. M. Chudakov, S. Lukyanov and V. V. Verkhusha. Photoactivatable fluorescent proteins. Nat. Rev. Mol. Cell Biol., 6(11):885–891, 2005.

[205] M. Andresen, M. C. Wahl, A. C. Stiel, F. Gräter, L. V. Schäfer, S. Trowitzsch, G. Weber, C. Eggeling, H. Grubmüller, S.W. Hell and S. Jakobs. Structure and mechanism of the reversible photoswitch of a fluorescent protein. Proc. Natl. Acad. Sci. USA, 102(37):13070– 13074, 2005.

[206] P. G.Wilmann, J. Petersen, R. J. Devenish, M. Prescott and J. Rossjohn. Variations on the GFP chromophore. J. Biol. Chem., 280(4):2401–2404, 2005.

[207] M. L. Quillin, D. A. Anstrom, X. K. Shu, S. O’Leary, K. Kallio, D. A. Chudakov and S. J. Remington. Kindling fluorescent protein from anemonia sulcata: Dark-state structure at 1.38 Å resolution. Biochemistry, 44(15):5774–5787, 2005.

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