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Angaben zur Quelle [Bearbeiten]

Autor     Martin Andresen, Markus C. Wahl, André C. Stiel, Frauke Gräter, Lars V. Schäfer, Simon Trowitzsch, Gert Weber, Christian Eggeling, Helmut Grubmüller, Stefan W. Hell, Stefan Jakobs
Titel    Structure and mechanism of the reversible photoswitch of a fluorescent protein
Zeitschrift    Proceedings of the National Academy of Sciences of the United States of America
Ausgabe    102
Jahr    2005
Nummer    37
Seiten    13070-13074
DOI    10.1073/pnas.0502772102
URL    http://www.pnas.org/content/102/37/13070.full.pdf

Literaturverz.   

yes
Fußnoten    yes
Fragmente    4


Fragmente der Quelle:
[1.] Tim/Fragment 013 12 - Diskussion
Zuletzt bearbeitet: 2014-11-27 22:14:55 Hindemith
Andresen et al 2005, Fragment, Gesichtet, KomplettPlagiat, SMWFragment, Schutzlevel sysop, Tim

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Seite: 13, Zeilen: 12-15
Quelle: Andresen et al 2005
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Recently, novel GFP-like fluorescent proteins have been discovered (Chudakov et al., 2003; Lukyanov et al. 2000; Ando et al., 2004) that can be reversibly photoswitched between a fluorescent (on) and nonfluorescent (off) state, that is, they are optically bistable and fluorescent. Recently, novel GFP-like fluorescent proteins have been discovered (4–6) that can be reversibly photoswitched between a fluorescent (on) and nonfluorescent (off) state, that is, they are optically bistable and fluorescent.

4. Ando, R., Mizuno, H. & Miyawaki, A. (2004) Science 306, 1370–1373.

5. Chudakov, D. M., Belousov, V. V., Zaraisky, A. G., Novoselov, V. V., Staroverov, D. B., Zorov, D. B., Lukyanov, S. & Lukyanov, K. A. (2003) Nat. Biotechnol. 21, 191–194.

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.

Anmerkungen

The source is given at the end of the next paragraph on the next page.

Sichter
(Hindemith), SleepyHollow02

[2.] Tim/Fragment 014 10 - Diskussion
Zuletzt bearbeitet: 2014-11-27 22:14:59 Hindemith
Andresen et al 2005, Fragment, Gesichtet, KomplettPlagiat, SMWFragment, Schutzlevel sysop, Tim

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Quelle: Andresen et al 2005
Seite(n): 13070, Zeilen: 44 ff.
asFP595 can be transferred by green light from a nonfluorescent off into a fluorescent on state from which it reverts back eventually, but this transition can also be promptly stimulated by gentle irradiation with blue light (Lukyanov et al., 2000). The "on-off" cycle can be repeated many times. However, with its low quantum yield (˂0.001), and comparatively slow switching kinetics, the photochromic properties of asFP595 are far from being optimal. It can be transferred by green light from a nonfluorescent off into a fluorescent on state from which it reverts back eventually, but this transition can also be promptly stimulated by gentle irradiation with blue light (6). The "on-off" cycle can be repeated many times. However, with its low quantum yield (<0.001, ref. 6) and comparatively slow switching kinetics, the photochromic properties of asFP595 are far from being optimal.

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.

Anmerkungen

The source is only mentioned in the next paragraph.

Sichter
(Hindemith), SleepyHollow02

[3.] Tim/Fragment 014 19 - Diskussion
Zuletzt bearbeitet: 2014-11-27 22:15:03 Hindemith
Andresen et al 2005, BauernOpfer, Fragment, Gesichtet, SMWFragment, Schutzlevel sysop, Tim

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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

[4.] Tim/Fragment 015 03 - Diskussion
Zuletzt bearbeitet: 2014-11-27 19:44:13 SleepyHollow02
Andresen et al 2005, Fragment, Gesichtet, KeineWertung, SMWFragment, Schutzlevel, Tim

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Quelle: Andresen et al 2005
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Andresen et al. (2005) indicated that the key event in asFP595 is a bottom hula twist (HTbot) mechanism resulting in a trans-cis isomerization of the chromophore. The chromophore on state is attributed to the cis conformation and in this conformation the chromophoric p-hydroxyphenyl group is likely to be in equilibrium between a (nonfluorescent) protonated and a (fluorescent) nonprotonated form (Chudakov et al., 2003). Our data indicate that the key event in asFP595 is a HTbot mechanism resulting in a trans-cis isomerization of the chromophore. The chromophore on state is attributed to the cis conformation.

[...] In the cis conformation, the chromophoric p-hydroxyphenyl group is likely to be in equilibrium between a (nonfluorescent) protonated and a (fluorescent) nonprotonated form (11).


11. Chudakov, D. M., Feofanov, A. V., Mudriku, N. N., Lukyanov, S. & Lukyanov, K. A. (2003) J. Biol. Chem. 278, 7215–7219.

Anmerkungen

The source is given, but the last sentence is attributed to Chudakov et al. (2003), but it is taken from the source including that reference.

Sichter
(Hindemith), SleepyHollow02

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