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| Untersuchte Arbeit: Seite: 7, Zeilen: 1 ff. (komplett) |
Quelle: Nienhaus 2006 Seite(n): 4212, 4213, Zeilen: 4212: l.col.: 30 ff.; 4213: l.col: 1ff |
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| [It consists of an imidazolinone ring generated by cyclization between the Gln63-C' and the Gly65-Nα atoms and the Tyr64] hydroxyphenyl group, which is made coplanar with the imidazolinone due to dehydrogenation insaturation of its Cα-Cβ bond. Whereas there is a glutamine in the first position of the tripeptide instead of the serine in AvGFP, the AsGFP chromophore is essentially identical to that of AvGFP, including the cis configuration at the Tyr64-Cβ, which is encountered more frequently than the trans conformation.
Fig. 2 (A) Top and (B) side view of the electron density map of the AsGFP chromophore and its environment, contoured at 1.2 s. (C) Close-up of the AsGFP chromophore (green, carbon; red, oxygen; blue, nitrogen) and surrounding residues (black, carbon; red, oxygen; blue, nitrogen). The backbone structures are plotted as lines; the side chains are accentuated. Water molecules are plotted as red spheres. Hydrogen bonds are represented by dashed lines. Distances are given in angstroms. (Nienhaus et al., 2006) The chromophore of AsGFP is tightly encased within the β-barrel by a hydrogen bond network involving polar and charged residues and altogether 10 structural waters within a distance of 5 Angstrom from the imidazolinone oxygen. |
Figure 1 (A) Top and (B) side view of the electron density map of the asFP499 chromophore and its environment, contoured at 1.2 s. (C) Close-up of the asFP499 chromophore (green, carbon; red, oxygen; blue, nitrogen) and surrounding residues (black, carbon; red, oxygen; blue, nitrogen). The backbone structures are plotted as lines; the side chains are accentuated. Water molecules are plotted as red spheres. Hydrogen bonds are represented by dashed lines. Distances are given in angstroms. It consists of an imidazolinone ring generated by cyclization between the Gln63-C´ and the Gly65-Nα atoms and the Tyr64 hydroxyphenyl group, which is made coplanar with the imidazolinone due to dehydrogenation insaturation of its Cα-Cβ bond. Whereas there is a glutamine in the first position of the tripeptide instead of the serine in avGFP, the asFP499 chromophore is essentially identical to that of avGFP, including the cis configuration at the Tyr64-Cβ, which is encountered more frequently than the trans conformation. The chromophore of asFP499 is tightly encased within the β-barrel by a hydrogen-bond network involving polar and charged residues and altogether 10 structural waters within a [page 4213] distance of 5 A° from the imidazolinone oxygen. |
The source is given for the figure and its caption, but not for the remainder of the text. |
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