Fandom

VroniPlag Wiki

Tim/008

< Tim

31.268Seiten in
diesem Wiki
Seite hinzufügen
Diskussion0 Share

Störung durch Adblocker erkannt!


Wikia ist eine gebührenfreie Seite, die sich durch Werbung finanziert. Benutzer, die Adblocker einsetzen, haben eine modifizierte Ansicht der Seite.

Wikia ist nicht verfügbar, wenn du weitere Modifikationen in dem Adblocker-Programm gemacht hast. Wenn du sie entfernst, dann wird die Seite ohne Probleme geladen.

Identification and characterization of Fluorescent Protein from marine organisms and potentially applications

von Dr. Tiziana Masullo

vorherige Seite | zur Übersichtsseite | folgende Seite
Statistik und Sichtungsnachweis dieser Seite findet sich am Artikelende
[1.] Tim/Fragment 008 01 - Diskussion
Zuletzt bearbeitet: 2014-10-25 05:59:20 Hindemith
BauernOpfer, Fragment, Gesichtet, Nienhaus 2006, SMWFragment, Schutzlevel sysop, Tim

Typus
BauernOpfer
Bearbeiter
SleepyHollow02
Gesichtet
Yes.png
Untersuchte Arbeit:
Seite: 8, Zeilen: 1-7
Quelle: Nienhaus 2006
Seite(n): 4213, Zeilen: l.col: 1 ff.
Figure 2 C displays the chromophore cage, with potential hydrogen-bond interactions represented by dashed lines. The highly conserved residues Arg92 and Glu212 have been implicated as being crucially involved in the mechanism of autocatalytic chromophore formation (Ormo et al., 1996; Sniegowski et al., 2005; Wood et al., 2005). The Arg92 guanidinium group hydrogen bonds to the Tyr64-derived carbonyl oxygen, whereas Glu212 is positioned within hydrogen-bonding distance to the heterocyclic ring nitrogen. Fig. 1 C displays the chromophore cage, with potential hydrogen-bond interactions represented by dashed lines. [...] The highly conserved residues Arg92 and Glu212 have been implicated as being crucially involved in the mechanism of autocatalytic chromophore formation (6,40,41). The Arg92 guanidinium group hydrogen bonds to the Tyr64-derived carbonyl oxygen, whereas Glu212 is positioned within hydrogen-bonding distance to the heterocyclic ring nitrogen, as has been observed earlier for yellow avGFP variants (42)

6. Ormo¨ , M., A. B. Cubitt, K. Kallio, L. A. Gross, R. Y. Tsien, and S. J. Remington. 1996. Crystal structure of the Aequorea victoria green fluorescent protein. Science. 273:1392–1395.

40. Sniegowski, J. A., J. W. Lappe, H. N. Patel, H. A. Huffman, and R. M. Wachter. 2005. Base catalysis of chromophore formation in Arg96 and Glu222 variants of green fluorescent protein. J. Biol. Chem. 280: 26248–26255.

41. Wood, T. I., D. P. Barondeau, C. Hitomi, C. J. Kassmann, J. A. Tainer, and E. D. Getzoff. 2005. Defining the role of arginine 96 in green fluorescent protein fluorophore biosynthesis. Biochemistry. 44:16211– 16220.

42. Wachter, R. M., M. A. Elsliger, K. Kallio, G. T. Hanson, and S. J. Remington. 1998. Structural basis of spectral shifts in the yellow-emission variants of green fluorescent protein. Structure. 6: 1267–1277.

Anmerkungen

The source is given the previous page to reference the figure that is described here. Nothing indicates, however, that this section is also taken from the source.

Sichter
(SleepyHollow02), Hindemith

[2.] Tim/Fragment 008 10 - Diskussion
Zuletzt bearbeitet: 2014-11-27 22:14:52 Hindemith
BauernOpfer, Fragment, Gesichtet, SMWFragment, Schutzlevel sysop, Tasdemir et al 2008, Tim

Typus
BauernOpfer
Bearbeiter
Hindemith
Gesichtet
Yes.png
Untersuchte Arbeit:
Seite: 8, Zeilen: 10-19
Quelle: Tasdemir et al 2008
Seite(n): 613, 621, Zeilen: 613: r. col: 9 ff.; 621: r.col: 17 ff.
Contrary to monomeric AvGFP, all known Anthozoa GFP-like proteins reported to date form oligomers and exist mostly as tetramers (Baird et al., 2000; Mizuno et al., 2001; Wiedenmann et al., 2002; Shagin et al., 2004). The oligomerisation does not impair their application as reporter genes, selection markers or biosensors, but limits their use as fusion tags to study, for instance, protein localization and dynamics in living cells (Baird et al., 2000; Lauf et al., 2001; Mizuno et al., 2001). A possible solution to this problem is the genetic engineering of the fluorescent protein of interest by mutagenesis, creating mutants that form functional monomeric variants. For example, Tasdemir et al. (2008) converted the tetrameric AsGFP into dimeric and monomeric variants guided by a rational strategy of sequence alignments. Contrary to monomeric AvGFP, all known Anthozoa GFP-like proteins reported to date form oligomers and exist mostly as tetramers (Baird et al., 2000; Vrzheshch et al., 2000; Mizuno et al., 2001; Wiedenmann et al., 2002; Shagin et al., 2004). The oligomerisation does not impair their application as reporter genes, selection markers or biosensors, but limits their use as fusion tags to study, for instance, protein localisation and dynamics in living cells (Baird et al., 2000; Lauf et al., 2001; Mizuno et al., 2001). A possible solution to this problem is the genetic engineering of the fluorescent protein (FP) of interest by mutagenesis, creating mutants that form functional monomeric variants.

[page 621]

In summary, the present investigations led to a successful conversion of tetrameric AsGFP499 into dimeric and monomeric variants guided by a rational strategy of sequence alignments.

Anmerkungen

The source is mentioned, but as an illustration ("For example [...]") of the previously said and not as a reference of a source for it.

Sichter
(Hindemith), SleepyHollow02

[3.] Tim/Fragment 008 21 - Diskussion
Zuletzt bearbeitet: 2014-10-24 20:10:07 Hindemith
BauernOpfer, Fragment, Gesichtet, SMWFragment, Schutzlevel sysop, Tim, Wiedenmann 2000

Typus
BauernOpfer
Bearbeiter
SleepyHollow02
Gesichtet
Yes.png
Untersuchte Arbeit:
Seite: 8, Zeilen: 21-28
Quelle: Wiedenmann 2000
Seite(n): 14092, Zeilen: l.col, last lines
Localization.

Because of their content of protein pigments, the tentacles of A. sulcata var. rufescens exhibit three hues under daylight conditions.

The upper side is green, the underside is orange, and the tips of tentacles show a vivid reddish color (fig. 3A).

The green and the orange pigments exhibit a bright fluorescence under irradiation with UV light at 366 nm (fig. 3B). The reddish protein of the tips is nonfluorescent. The protein pigments all are located in the ectoderm of the tentacles (fig. 3C).

Localization. Because of their content of protein pigments, the tentacles of A. sulcata var. rufescens exhibit three hues under daylight conditions. The upper side is green, the underside is orange, and the tips of tentacles show a vivid reddish color (Fig. 1A). The green and the orange pigments exhibit a bright fluorescence under irradiation with UV light at 366 nm (Fig. 1B). In a few specimens, two opposite spots at the mouth and the verrucae of the column also fluoresce in orange. The reddish protein of the tips is nonfluorescent. The protein pigments all are located in the ectoderm of the tentacles (Fig. 1C).
Anmerkungen

The source is mentioned on the following pages, but there is no indication that this passage is also taken from it.

Sichter
(SleepyHollow02), Hindemith


vorherige Seite | zur Übersichtsseite | folgende Seite
Letzte Bearbeitung dieser Seite: durch Benutzer:Hindemith, Zeitstempel: 20141127222131

Auch bei Fandom

Zufälliges Wiki