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Angaben zur Quelle [Bearbeiten]

Autor     Richard R. Chapleau, Rebecca Blomberg, Peter C. Ford, Martin Sagermann
Titel    Design of a highly specific and noninvasive biosensor suitable for real-time in vivo imaging of mercury (II) uptake
Zeitschrift    Protein Science
Jahr    2008
Seiten    614–622
URL    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2271171/pdf/614.pdf

Literaturverz.   

yes
Fußnoten    yes
Fragmente    2


Fragmente der Quelle:
[1.] Tim/Fragment 018 17 - Diskussion
Zuletzt bearbeitet: 2014-11-27 22:26:26 Hindemith
Chapleau 2008, Fragment, KeineWertung, SMWFragment, Schutzlevel, Tim, ZuSichten

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Seite: 18, Zeilen: 17-31
Quelle: Chapleau 2008
Seite(n): 614, Zeilen: abstract
In their study, Chapleau et al. (2008) presented a novel fluorescence-based biosensor for the direct monitoring of the uptake and distribution of Hg under noninvasive in vivo conditions. With the introduction of a cysteine residue at position 205, AvGFP was converted into a highly specific biosensor for this metal ion. The binding of mercury to sulfhydryl groups in proteins is extremely efficient and is likely to be the main cause for its toxicity. The mutant protein exhibited a dramatic absorbance and fluorescence change upon mercuration at neutral pH (fig. 10). Absorbance and fluorescence properties with respect to the metal concentration exhibited sigmoidal binding behavior with a detection limit in the low nM range. At very high concentrations of mercury (>200 mM), fluorescence of all tested eGFP variants vanished completely. Treatment with metal-binding agents such as β-mercaptoethanol, glutathione, or EDTA did not regenerated the fluorescence of the protein, suggesting tight binding of the metal to the protein under these conditions. The crystal structures obtained of mutant eGFP205C indicate a possible access route of the metal into the core of the protein. Cysteine 205C is located in close proximity to the hydroxyl group of the chromophore tyrosine. In this study, a novel fluorescence-based biosensor is presented that allows for the direct monitoring of the uptake and distribution of the metal under noninvasive in vivo conditions. With the introduction of a cysteine residue at position 205, located in close proximity to the chromophore, the green fluorescent protein (GFP) from Aequorea victoria was converted into a highly specific biosensor for this metal ion. The mutant protein exhibits a dramatic absorbance and fluorescence change upon mercuration at neutral pH. Absorbance and fluorescence properties with respect to the metal concentration exhibit sigmoidal binding behavior with a detection limit in the low nanomolar range. Time-resolved binding studies indicate rapid subsecond binding of the metal to the protein. The crystal structures obtained of mutant eGFP205C indicate a possible access route of the metal into the core of the protein.
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Sichter

[2.] Tim/Fragment 019 01 - Diskussion
Zuletzt bearbeitet: 2014-10-15 18:50:19 Singulus
Chapleau 2008, Fragment, Gesichtet, SMWFragment, Schutzlevel sysop, Tim, Verschleierung

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Untersuchte Arbeit:
Seite: 19, Zeilen: 1-2
Quelle: Chapleau 2008
Seite(n): 619, Zeilen: l.col.: 14 ff.
Previous studies have suggested that the irregular conformation of the structure might allow solutes to penetrate into the core of the protein (Agmon, 2005). Previous studies have suggested that the irregular conformation of the structure might allow solutes to penetrate into the core of the protein (Agmon 2005).
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