Biology Reference
In-Depth Information
The situation is slightly different for the red- and orange-fluorescent proteins.
Comparative studies are widely missing and, therefore, the mutations which influ-
ence t Fl are almost unknown. Even the general decay mechanisms are not yet
described. The timescale of their biotechnological evolution can be roughly esti-
mated to be a decade, based on the previous developments with avFPs. We expect
that orange and red FPs will be improved with respect to t Fl and F Fl once the most
appropriate candidates for imaging purposes are identified.
Acknowledgements This work was supported by the German Science Foundation (DFG JU650/
2-2). We are indebted to Nediljko Budisa for the generous gift of proteins with unnatural amino
acids. We also thank Dagmar Auerbach for careful proofreading.
References
1. Kummer AD, Kompa C, Niwa H, Hirano T, Kojima S, Michel-Beyerle ME (2002) Viscosity-
dependent fluorescence decay of the GFP chromophore in solution due to fast internal
conversion. J Phys Chem B 106:7557-7559
2. Lammich L, Petersen MA, Brøndsted NM, Andersen LH (2007) The gas-phase absorption
spectrum of a neutral GFP model chromophore. Biophys J 92:201-207
3. Litvinenko KL, Webber NM, Meech SR (2003) Internal conversion in the chromophore of
the green fluorescent protein: temperature dependence and isoviscosity analysis. J Phys
Chem A 107:2616-2623
4. Kojima S, Hirano T, Niwa H, Ohashi M, Inouye S, Tsuji FI (1997) Mechanism of the redox
reaction of the Aequorea green fluorescent protein (GFP). Tetrahedron Lett 38:2875-2878
5. Inouye S, Tsuji FI (1994) Evidence for redox forms of the Aequorea green fluorescent
protein. FEBS Lett 351:211-214
6. Drobizhev M, Tillo S, Makarov NS, Hughes TE, Rebane A (2009) Absolute two-photon
absorption spectra and two-photon brightness of orange and red fluorescent proteins. J Phys
Chem 113:855-859
7. Nifosi R, Luo Y (2007) Predictions of novel two-photon absorption bands in fluorescent
proteins. J Phys Chem B 111:14043-14050
8. Tillo SE, Hughes TE, Makarov NS, Rebane A, Drobizhev M (2010) A new approach to dual-
color two-photon microscopy with fluorescent proteins. BMC Biotechnol 10:6
9. Langhojer F, Dimler F, Jung G, Brixner T (2009) Ultrafast photoconversion of the green
fluorescent protein studied by accumulative femtosecond spectroscopy. Biophys
J
96:2763-2770
10. van Thor JJ, Gensch T, Hellingwerf KJ, Johnson LN (2002) Phototransformation of green
fluorescent protein with UV and visible light leads to decarboxylation of glutamate 222. Nat
Struct Biol 9:37-41
11. Hell SW (2007) Far-field optical nanoscopy. Science 316:1153-1158
12. Klar TA, Jakobs S, Dyba M, Egner A, Hell SW (2000) Fluorescence microscopy with
diffraction resolution limit broken by stimulated emission. Proc Natl Acad Sci USA
97:8206-8210
13. Widengren J, Mets U, Rigler R (1999) Photodynamic properties of green fluorescent proteins
investigated by fluorescence correlation spectroscopy. Chem Phys 250:171-186
14. Jim ´ nez-Banzo A, Nonell S, Hofkens J, Flors C (2008) Singlet oxygen photosensitization by
EGFP and its chromophore HBDI. Biophys J 94:168-172
15. Bulina ME, Chudakov DM, Britanova OV, Yanushevich YG, Staroverov DB, Chepurnykh
TV, Merzlyak EM, Shkrob MA, Lukyanov S, Lukyanov KA (2006) A genetically encoded
photosensitizer. Nat Biotechnol 24:95-99
Search WWH ::




Custom Search