Green Fluorescent Protein: Difference between revisions
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m →The Chromophore: added Fang et al 2009 paper where GFP was on the cover |
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This quandary led Phillips to study the acid/base chemistry catalyzing the initial cyclization of the chromophore. He found that Arg<sup>96</sup> actually acts as a | This quandary led Phillips to study the acid/base chemistry catalyzing the initial cyclization of the chromophore. He found that Arg<sup>96</sup> actually acts as a | ||
<scene name='Green_Fluorescent_Protein/Arg96/1' target='3' >base</scene> by withdrawing electrons through hydrogen bonding with the carbonyl oxygen of Ser<sup>65</sup> to activate the carbonyl carbon for nucleophilic attack by the amide nitrogen of Gly<sup>67</sup>. This mechanism was further supported by ''ab initio'' calculations, as well as database searches of similar compounds and protein sequences. Through acid/base chemistry, the chromophore is stabilized by resonance.<ref name="Phillips" /> | <scene name='Green_Fluorescent_Protein/Arg96/1' target='3' >base</scene> by withdrawing electrons through hydrogen bonding with the carbonyl oxygen of Ser<sup>65</sup> to activate the carbonyl carbon for nucleophilic attack by the amide nitrogen of Gly<sup>67</sup>. This mechanism was further supported by ''ab initio'' calculations, as well as database searches of similar compounds and protein sequences. Through acid/base chemistry, the chromophore is stabilized by resonance.<ref name="Phillips" /> Femtosecond Raman spectroscopy has been used to map the alteration of the structure close the chromophore during excited-state protein transfer and shown that chromophore wagging is orchestated by the protein environment.<ref name="Fang">PMID: 19907490</ref> | ||
===Mutant Studies=== | ===Mutant Studies=== | ||
