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Angaben zur Quelle [Bearbeiten]

Autor     Yasmeen Rahimi, Ann Goulding, Suresh Shrestha, Sweetie Mirpuri, Sapna K. Deo
Titel    Mechanism of Copper Induced Fluorescence Quenching of Red Fluorescent Protein, DsRed
Zeitschrift    Biochemical and Biophysical Research Communications
Ausgabe    370
Datum    May 2008
Nummer    1
Seiten    57-61
Anmerkung    The linked file has page numbers 1-13. Those are used for the documentation.
DOI    10.1016/j.bbrc.2008.03.034
URL    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2527065/pdf/nihms49229.pdf

Literaturverz.   

yes
Fußnoten    yes
Fragmente    2


Fragmente der Quelle:
[1.] Tim/Fragment 022 06 - Diskussion
Zuletzt bearbeitet: 2014-11-27 19:30:27 SleepyHollow02
Fragment, Gesichtet, KeineWertung, Rahimi et al 2008, SMWFragment, Schutzlevel, Tim

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Bearbeiter
Hindemith
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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

[2.] Tim/Fragment 071 05 - Diskussion
Zuletzt bearbeitet: 2014-11-27 22:14:45 Hindemith
BauernOpfer, Fragment, Gesichtet, Rahimi et al 2008, SMWFragment, Schutzlevel sysop, Tim

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Untersuchte Arbeit:
Seite: 71, Zeilen: 5-14
Quelle: Rahimi et al 2008
Seite(n): 5, Zeilen: 15 ff.
It is known that in the case of proteins only the fluorophores located at the surface can be dynamically quenched whereas the internal fluorophores are quenched by static process due to higher hydrophobicity in the interior. In the case of AsGFP, the chromophore is well shielded inside a β-barrel and hence is not accessible for dynamic or collisional quenching. Rahimi et al. (2008) reported for DsRed, that Cu2+ forms a complex with specific amino acids on the protein. This complex formation can lead to formation of non-fluorescent species in three ways, i) by affecting hydrogen-bonding network of the chromophore, ii) by bringing Cu2+ close to chromophore such that it contacts the excited-state of the chromophore, iii) by causing conformation/structural changes in the protein. It is known that in the case of proteins only the fluorophores located at the surface can be dynamically quenched whereas the internal fluorophores are quenched by static process due to higher hydrophobicity in the interior. In the case of DsRed, the chromophore is well shielded inside a β-barrel and hence is not accessible for dynamic or collisional quenching. [...] We hypothesize that, in DsRed, Cu2+ forms a complex with specific amino acids on the protein. This complex formation can lead to formation of non-fluorescent species in three ways, i) by affecting hydrogen-bonding network of the chromophore, ii) by bringing Cu2+ close to chromophore such that it contacts the excited-state of the chromophore, iii) by causing conformation/structural changes in the protein.
Anmerkungen

The source is mentioned in the middle. The reader might assume that the text following the reference is close to the source, but would expect that the text before the reference is the view of the author.

It is remarkable that Rahmini et al. (2008) "hypothesize that, in DsRed, Cu2+ forms a complex with specific amino acids on the protein", whereas T. M. writes: "Rahimi et al. (2008) reported for DsRed, that Cu2+ forms a complex with specific amino acids on the protein." From a scientific point of view, this is a significant misrepresentation.

Sichter
(Hindemith), SleepyHollow02

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