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[1.] Tim/Fragment 018 17 - Diskussion
Bearbeitet: 27. November 2014, 22:26 (Hindemith)
Erstellt: 7. October 2014, 06:14 SleepyHollow02
Chapleau 2008, Fragment, KeineWertung, SMWFragment, Schutzlevel, Tim, ZuSichten

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SleepyHollow02
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Untersuchte Arbeit:
Seite: 18, Zeilen: 17-31
Quelle: Chapleau 2008
Seite(n): 614, Zeilen: abstract
In their study, Chapleau et al. (2008) presented a novel fluorescence-based biosensor for the direct monitoring of the uptake and distribution of Hg under noninvasive in vivo conditions. With the introduction of a cysteine residue at position 205, AvGFP was converted into a highly specific biosensor for this metal ion. The binding of mercury to sulfhydryl groups in proteins is extremely efficient and is likely to be the main cause for its toxicity. The mutant protein exhibited a dramatic absorbance and fluorescence change upon mercuration at neutral pH (fig. 10). Absorbance and fluorescence properties with respect to the metal concentration exhibited sigmoidal binding behavior with a detection limit in the low nM range. At very high concentrations of mercury (>200 mM), fluorescence of all tested eGFP variants vanished completely. Treatment with metal-binding agents such as β-mercaptoethanol, glutathione, or EDTA did not regenerated the fluorescence of the protein, suggesting tight binding of the metal to the protein under these conditions. The crystal structures obtained of mutant eGFP205C indicate a possible access route of the metal into the core of the protein. Cysteine 205C is located in close proximity to the hydroxyl group of the chromophore tyrosine. In this study, a novel fluorescence-based biosensor is presented that allows for the direct monitoring of the uptake and distribution of the metal under noninvasive in vivo conditions. With the introduction of a cysteine residue at position 205, located in close proximity to the chromophore, the green fluorescent protein (GFP) from Aequorea victoria was converted into a highly specific biosensor for this metal ion. The mutant protein exhibits a dramatic absorbance and fluorescence change upon mercuration at neutral pH. Absorbance and fluorescence properties with respect to the metal concentration exhibit sigmoidal binding behavior with a detection limit in the low nanomolar range. Time-resolved binding studies indicate rapid subsecond binding of the metal to the protein. The crystal structures obtained of mutant eGFP205C indicate a possible access route of the metal into the core of the protein.
Anmerkungen

The source is mentioned and it is not a verbatim copy.

Sichter

[2.] Tim/Fragment 005 05 - Diskussion
Bearbeitet: 25. October 2014, 05:41 (Hindemith)
Erstellt: 7. October 2014, 09:11 SleepyHollow02
Fragment, KeineWertung, SMWFragment, Schutzlevel sysop, Tim, Wiedenmann 2000, ZuSichten

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SleepyHollow02, Hindemith
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Untersuchte Arbeit:
Seite: 5, Zeilen: 5-12
Quelle: Wiedenmann 2000
Seite(n): 14091, Zeilen: l.col.: 30 ff.
Mainly green and orange fluorescence from unidentified pigments was described for various no bioluminescent cnidarians (Catala, 1959; Kawaguti, 1944, 1966; Schlichter et al., 1986, 1988; Mazel, 1995, 1997; Doubilet, 1997). The green and orange fluorescent pigments were found in the color morphs of the Mediterranean sea anemone A. sulcata revealed quite similar properties as GFP from A. victoria. Many authors have found that the tentacles of this species exhibit a bright green and orange fluorescence and a nonfluorescent reddish color in the tips of its tentacles and the exclusive expression of GFPs in the ectoderm of the tentacles (Wiedenmann et al., 2000, Leutenegger et al., 2007) determined that AsGFP contributed ~ 5% to the total soluble cellular protein of non-bleached individuals. Mainly green and orange fluorescence from unidentified pigments was described for various nonbioluminescent cnidarians (13–20). The green and orange fluorescent pigments we found in the color morphs of the Mediterranean sea anemone Anemonia sulcata revealed quite similar properties as GFP from A. victoria. [...] Most recently, this view was confirmed by the cloning of six fluorescent proteins from nonbioluminescent Anthozoa homologous to the GFP from A. victoria (22).

Our interest was focused on the morph var. rufescens of A. sulcata (23). The tentacles of this morph exhibit a bright green and orange fluorescence and a nonfluorescent reddish color in the tips of its tentacles.


14. Kawaguti, S. (1944) Palao. Trop. Biol. Stn. Stud. 2, 617–674.

15. Kawaguti, S. (1966) Biol. J. Okayama Univ. 2, 11–21.

16. Schlichter, D., Fricke, H. W. & Weber, W. (1986) Mar. Biol. 91, 403–407.

17. Schlichter, D., Fricke, H. W. & Weber, W. (1988) Endocyt. C. Res. 5, 83–94.

18. Mazel, C. H. (1995) Mar. Ecol. Prog. Ser. 120, 185–191.

19. Mazel, C. H. (1997) Ocean Optics XIII SPIE 2963, 240–245.

20. Doubilet, P. (1997) Nat. Geogr. 192, 32–43.

22. Matz, M. V., Fradkov, A. F., Labas, Y. A., Savitsky, A. P., Zaraisky, A. G., Markelov, M. L. & Lukyanov, S. A. (1999) Nat. Biotechnol. 17, 969–973.

23. Andres, A. (1883) in Accademia dei lincei, ed. Atti, R. (Rendicont, Rome), pp. 211–674.

Anmerkungen

The source is mentioned, but the extent of the copying (which includes 7 references to the literature) doen't become clear to the reader.

Sichter
(SleepyHollow02), (Hindemith)

[3.] Tim/Fragment 014 13 - Diskussion
Bearbeitet: 25. October 2014, 13:07 (Hindemith)
Erstellt: 25. October 2014, 13:03 Hindemith
Fragment, KeineWertung, SMWFragment, Schaefer 2007b, Schutzlevel, Tim, ZuSichten

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KeineWertung
Bearbeiter
Hindemith
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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.

Anmerkungen

The source is not mentioned.

Sichter
(Hindemith)

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