Sandbox 719: Difference between revisions
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==== The Chromophore environment ==== | ==== The Chromophore environment ==== | ||
<Structure load='1G7K' size=' | <Structure load='1G7K' size='470' frame='true' align='left' scene='Insert optional scene name here' /> | ||
[[Image:Chromophore1G7K.gif |250px|right|thumb|Chromophore of the DsRed protein]] | [[Image:Chromophore1G7K.gif |250px|right|thumb|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 -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. | ||
