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Typus
BauernOpfer
Bearbeiter
Hindemith
Gesichtet
Yes.png
Untersuchte Arbeit:
Seite: 14, Zeilen: 19-24, 27-33
Quelle: Andresen et al 2005
Seite(n): 13071, Zeilen: r.col. 14 ff.
The quantum yield of these variants was major as compared with that of the wt asFP595 protein. As in all GFP-like proteins, the asFP595 chromophore resides in a helical segment, which is enclosed in an 11-stranded β-barrel (Ormo et al., 1996; Wall et al., 2000; Yang et al., 1996). The tripeptide M63-Y64-G65 rearranges to a chromophoric, conjugated 2-iminomethyl-5-(4-hydroxybenzylidene) imidazolinone (MYG) system.

[...]

Unlike most other GFP-like proteins, the protein backbone is broken between C62 and the chromophore. Nevertheless, the former M63 Cα and backbone nitrogen atoms are in plane with the imidazolinone ring and, thus, part of the conjugated system. The imino group expands the conjugated system of MYG, likely accounting for the shift of the absorption maximum toward a longer wavelength (572 nm) as compared with that of GFP (470 nm). The MYG chromophore of the off state asFP595 exclusively adopts the trans conformation.

As in all GFP-like proteins, the asFP595 chromophore resides in a helical segment, which is enclosed in an 11-stranded β-barrel (20–23). The tripeptide M63-Y64-G65 rearranges to a chromophoric, conjugated 2-iminomethyl-5-(4-hydroxybenzylidene) imidazolinone (MYG) system, in agreement with previous biochemical analysis of proteolytic peptides (24). Unlike most other GFP-like proteins, the protein backbone is broken between C62 and the chromophore. Nevertheless, the former M63 Cα and backbone nitrogen atoms are in plane with the imidazolinone ring and, thus, part of the conjugated system. The imino group expands the conjugated system of MYG, likely accounting for the shift of the absorption maximum toward a longer wavelength (572 nm) as compared with that of GFP (470 nm). The MYG chromophore of the off state asFP595 exclusively adopts the trans conformation.

[...]

[...] This variant has 12 times the fluorescence quantum yield as compared with that of the wt asFP595 protein (6).


6. Lukyanov, K. A., Fradkov, A. F., Gurskaya, N. G., Matz, M. V., Labas, Y. A., Savitsky, A. P., Markelov, M. L., Zaraisky, A. G., Zhao, X. N., Fang, Y., et al. (2000) J. Biol. Chem. 275, 25879–25882.

20. Ormo, M., Cubitt, A. B., Kallio, K., Gross, L. A., Tsien, R. Y. & Remington, S. J. (1996) Science 273, 1392–1395.

21. Wall, M. A., Socolich, M. & Ranganathan, R. (2000) Nat. Struct. Biol. 7, 1133–1138.

22. Yang, F., Moss, L. G. & Phillips, G. N., Jr. (1996) Nat. Biotechnol. 14, 1246–1251.

23. Yarbrough, D., Wachter, R. M., Kallio, K., Matz, M. V. & Remington, S. J. (2001) Proc. Natl. Acad. Sci. USA. 98, 462–467.

24. Zagranichny, V. E., Rudenko, N. V., Gorokhovatsky, A. Y., Zakharov, M. V., Balashova, T. A. & Arseniev, A. S. (2004) Biochemistry 43, 13598– 13603.

Anmerkungen

The source is mentioned right before the documented passage. One could assume that the first documented sentence describes the results of Andresen et al. (2005), what follows, however, is attributed to other sources.

Sichter
(Hindemith), SleepyHollow02

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