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3 gesichtete Fragmente: "Verdächtig" oder "Keine Wertung"

[1.] Tim/Fragment 018 01 - Diskussion
Bearbeitet: 27. October 2014, 05:00 (Hindemith)
Erstellt: 8. October 2014, 08:37 SleepyHollow02
Fragment, Gesichtet, Isarankura 2009, KeineWertung, SMWFragment, Schutzlevel sysop, Tim

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SleepyHollow02
Gesichtet
Yes.png
Untersuchte Arbeit:
Seite: 18, Zeilen: 1-3
Quelle: Isarankura 2009
Seite(n): 353, Zeilen: 18ff
[These] include the green fluorescent protein and its variants, the red fluorescent protein (DsRed) from the tropical coral namely Discosoma sp.

Richmond et al. (2000) have introduced metal-binding sites onto the surface of GFP and found that these metal-binding mutants of GFP exhibited fluorescence quenching at lower transition metal ion (Cu2+, Ni2+, or Co2+) concentrations (104) than those of the wild-type protein.

These include the green fluorescent protein (GFP) and its variants from the Pacific Northwest jellyfish namely Aequorea victoria [7–11], the red fluorescent protein (DsRed) from the tropical coral namely Discosoma sp. [12–14], and the far-red fluorescent (HcRed) protein from the reef coral namely Heteractis crispa [15, 16].

[...] By the same year, Richmond and his colleagues have introduced metal-binding sites onto the surface of GFP and found that metals in close proximity to chromophores are known to quench fluorescence in a distance-dependent fashion [8].

Anmerkungen

The copied text starts on the previous page: Tim/Fragment 017 15‎

The source is not mentioned here. It will be mentioned on page 19.

Sichter
(SleepyHollow02), Hindemith

[2.] Tim/Fragment 022 06 - Diskussion
Bearbeitet: 27. November 2014, 19:30 (SleepyHollow02)
Erstellt: 8. October 2014, 11:16 Hindemith
Fragment, Gesichtet, KeineWertung, Rahimi et al 2008, SMWFragment, Schutzlevel, Tim

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Hindemith
Gesichtet
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Untersuchte Arbeit:
Seite: 22, Zeilen: 6-13
Quelle: Rahimi et al 2008
Seite(n): 1, Zeilen: 13 ff.
Rahimi et al. (2008) have performed spectroscopic investigations to determine the mechanism of quenching of DsRed mutants fluorescence in the presence of Cu2+. Stern-Volmer constants and quenching rate constants supported the observation of static quenching in DsRed in the presence of Cu2+. Circular dichroism (CD)-spectroscopic studies revealed no effect of Cu2+-binding on the secondary structure or conformation of the protein. The effect of pH changes on the quenching of DsRed fluorescence in the presence of copper resulted in pKa values indicative of histidine and cysteine residue involvement in Cu2+ binding. In this work, we have performed spectroscopic investigations to determine the mechanism of quenching of DsRed fluorescence in the presence of Cu2+. [...] Stern-Volmer constants and quenching rate constants support the observation of static quenching in DsRed in the presence of Cu2+. Circular dichroism (CD)-spectroscopic studies revealed no effect of Cu2+-binding on the secondary structure or conformation of the protein. The effect of pH changes on the quenching of DsRed fluorescence in the presence of copper resulted in pKa values indicative of histidine and cysteine residue involvement in Cu2+ binding.
Anmerkungen

The source is given, but there is no indication that the copy is literal.

Sichter
(Hindemith), SleepyHollow02

[3.] Tim/Fragment 015 03 - Diskussion
Bearbeitet: 27. November 2014, 19:44 (SleepyHollow02)
Erstellt: 25. October 2014, 12:44 Hindemith
Andresen et al 2005, Fragment, Gesichtet, KeineWertung, SMWFragment, Schutzlevel, Tim

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Hindemith
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Untersuchte Arbeit:
Seite: 15, Zeilen: 3-8
Quelle: Andresen et al 2005
Seite(n): 13074, Zeilen: r.col: 12 ff.
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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