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Typus
BauernOpfer
Bearbeiter
SleepyHollow02
Gesichtet
Yes.png
Untersuchte Arbeit:
Seite: 6, Zeilen: 1-3, 4-15
Quelle: Nienhaus 2006
Seite(n): 4211 , 4212, Zeilen: 4211: l.col., 3 ff.; 4212 l.col. 11 ff.
[Nienhaus et al. (2006) described the quaternary structure and found that the asymmetric unit of AsGFP contains two identical tetramers related by a no crystallographic symmetry. They are arranged as dimers of dimers, so that two types of subunit interfaces can be distinguished; they are denoted as antiparallel (between subunits A/B] and C/D) and perpendicular (between subunits A/C and B/D) interfaces according to the mutual orientations of the main axes of the β-barrels. Both interfaces involve hydrophobic and hydrophilic interactions (fig. 1).

[...]

Relatively at tertiary structure, the monomeric subunits within the tetramers are essentially identical. The overall backbone topology shows the typical 11-stranded b-barrel [sic] fold, with the central a-helix [sic] interrupted by the chromophore. The N-terminal end (residues 1–7) forms a lid on the same barrel, thereby assisting in shielding the interior of the can from the environment, whereas the C-terminal tail (residues 220–228) wraps around the other barrel in the A/B dimer. The AsGFP structure is similar to that of AvGFP. Backbone structural differences between AsGFP and AvGFP are most pronounced in the region corresponding to amino acids 138–141 (143–146 in AvGFP) and in the loop region formed by amino acids 195–206 (204–216 in AvGFP).

The chromophore of AsGFP is a planar resonance system formed autocatalytically by residues Gln63, Tyr64, and Gly65 (fig. 2, A and B). It consists of an imidazolinone ring generated by cyclization between the Gln63-C' and the Gly65-Nα atoms and the Tyr64 [7 hydroxyphenyl group, which is made coplanar with the imidazolinone due to dehydrogenation insaturation of its Cα-Cβ bond.]

The asymmetric unit of asFP499 contains two identical tetramers related by a noncrystallographic symmetry. They are arranged as dimers of dimers, so that two types of subunit interfaces can be distinguished; they are denoted as antiparallel (between subunits A/B and C/D) and perpendicular (between subunits A/C and B/D) interfaces according to the mutual orientations of the main axes of the β-barrels. Both interfaces involve hydrophobic and hydrophilic interactions.

[page 4212]

Tertiary structure

The monomeric subunits within the tetramers are essentially identical, as judged from the average root mean-square deviation (rmsd) of the Ca atoms of 0.21 A° . The overall backbone topology shows the typical 11-stranded β-barrel fold, with the central α-helix interrupted by the chromophore. The N-terminal end (residues 1–7) forms a lid on the same barrel, thereby assisting in shielding the interior of the can from the environment, whereas the C-terminal tail (residues 220–228) wraps around the other barrel in the A/B dimer. The asFP499 structure is similar to that of avGFP, with an rmsd of the Ca atoms of 1.15A° . Backbone structural differences between asFP499 and avGFP are most pronounced in the region corresponding to amino acids 138–141 (143–146 in avGFP) and in the loop region formed by amino acids 195–206 (204–216 in avGFP).

The chromophore and its environment

The chromophore of asFP499 is a planar resonance system formed autocatalytically by residues Gln63, Tyr64, and Gly65 (Fig. 1, A and B). It consists of an imidazolinone ring generated by cyclization between the Gln63-C9 and the Gly65-Nα atoms and the Tyr64 hydroxyphenyl group, which is made coplanar with the imidazolinone due to dehydrogenation insaturation of itsCα-Cβ bond.

Anmerkungen

The source is mentioned once in the beginning. However, it does not become clear that the entire page (except the figure 1) is copied and that the copy is almost literal.

Sichter
(SleepyHollow02), Hindemith

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