Sandbox 719: Difference between revisions

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[[Image:Chromophore1G7K.gif |250px|right|thumb|Figure 2: Chromophore of the DsRed protein]]

Structure of the chromophore was predicted by sequence comparisons. Chromophore of the DsRed is localized in a very polar cavity, and results to the autocatalytic cyclization and hydrogenation of the -Gln66-Tyr67-Gly68- tripeptide. Environment of DsRed chromophore is much more complicated in DsRd than in GFP, cause to the hydrogen bond and salt bridge network. There more charges in DsRed than in GFP, due to three lysine (residues 70,83 and 163) and glutamic acid (residue 148) wich interact very closely with the chromophore. These charges are localized in two perpendicular band : the positive one is parallel to the axis of the chromophore, and the negative one perpendicular to this axis.

Structure of the chromophore was predicted by sequence comparisons. Chromophore of the DsRed is localized in a very polar cavity, and results to the autocatalytic cyclization and hydrogenation of the<scene name='Sandbox_719/Chromophore/1'> -Gln66-Tyr67-Gly68- tripeptide</scene>. Environment of DsRed chromophore is much more complicated in DsRd than in GFP, cause to the hydrogen bond and salt bridge network. There more charges in DsRed than in GFP, due to three lysine (residues 70,83 and 163) and glutamic acid (residue 148) wich interact very closely with the chromophore. These charges are localized in two perpendicular band : the positive one is parallel to the axis of the chromophore, and the negative one perpendicular to this axis.

The Phenolate oxygen of the chromophore forms a hydrogen bond with Ser-146 and a nearly water molecule, and it also forms a charge-charge with the Lys-163 residue. To forms all these interactions, the necessarily always charged.

There is an other important residue in the struture of the chromophore, the residue Glu-215 (equivalent to the residue Glu-222 in GFP). This residue is highly close to the chromophore, and it also interacts with a water molecule localized near GLN-66. But Glu-215 also interacts with the positively charged chain of Lys-70, and it forms a hydrogen with Ser-205 side chain, like in GFP.

Sandbox 719: Difference between revisions

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 <Structure load='1G7K' size='470' frame='true' align='left' scene='Insert optional scene name here' />
 [[Image:Chromophore1G7K.gif |250px|right|thumb|Figure 2: Chromophore of the DsRed protein]]
-Structure of the chromophore was predicted by sequence comparisons. Chromophore of the DsRed is localized in a very polar cavity, and results to the autocatalytic cyclization and hydrogenation of the -Gln66-Tyr67-Gly68- tripeptide. Environment of DsRed chromophore is much more complicated in DsRd than in GFP, cause to the hydrogen bond and salt bridge network. There more charges in DsRed than in GFP, due to three lysine (residues 70,83 and 163) and glutamic acid (residue 148) wich interact very closely with the chromophore. These charges are localized in two perpendicular band : the positive one is parallel to the axis of the chromophore, and the negative one perpendicular to this axis.
+Structure of the chromophore was predicted by sequence comparisons. Chromophore of the DsRed is localized in a very polar cavity, and results to the autocatalytic cyclization and hydrogenation of the<scene name='Sandbox_719/Chromophore/1'> -Gln66-Tyr67-Gly68- tripeptide</scene>. Environment of DsRed chromophore is much more complicated in DsRd than in GFP, cause to the hydrogen bond and salt bridge network. There more charges in DsRed than in GFP, due to three lysine (residues 70,83 and 163) and glutamic acid (residue 148) wich interact very closely with the chromophore. These charges are localized in two perpendicular band : the positive one is parallel to the axis of the chromophore, and the negative one perpendicular to this axis.
 The Phenolate oxygen of the chromophore forms a hydrogen bond with Ser-146 and a nearly water molecule, and it also forms a charge-charge with the Lys-163 residue. To forms all these interactions, the necessarily always charged.
 There is an other important residue in the struture of the chromophore, the residue Glu-215 (equivalent to the residue Glu-222 in GFP). This residue is highly close to the chromophore, and it also interacts with a water molecule localized near GLN-66. But Glu-215 also interacts with the positively charged chain of Lys-70, and it forms a hydrogen with Ser-205 side chain, like in GFP.