2pox: Difference between revisions

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==Overview==

Dronpa is a novel GFP-like fluorescent protein with exceptional, light-controlled switching properties. It may be reversibly switched, between a fluorescent on-state and a nonfluorescent off-state by, irradiation with light. To elucidate the molecular basis of the switching, mechanism, we generated reversibly switchable Dronpa protein crystals., Using these crystals we determined the elusive dark-state structure of, Dronpa at 1.95-A resolution. We found that the photoswitching results in a, cis-trans isomerization of the chromophore accompanied by complex, structural rearrangements of four nearby amino acid residues. Because of, this cascade of intramolecular events, the chromophore is exposed to, distinct electrostatic surface potentials, which are likely to influence, the protonation equilibria at the chromophore. We suggest a comprehensive, model for the light-induced switching mechanism, connecting a cascade of, structural rearrangements with different protonation states of the, chromophore.

Dronpa is a novel GFP-like fluorescent protein with exceptional light-controlled switching properties. It may be reversibly switched between a fluorescent on-state and a nonfluorescent off-state by irradiation with light. To elucidate the molecular basis of the switching mechanism, we generated reversibly switchable Dronpa protein crystals. Using these crystals we determined the elusive dark-state structure of Dronpa at 1.95-A resolution. We found that the photoswitching results in a cis-trans isomerization of the chromophore accompanied by complex structural rearrangements of four nearby amino acid residues. Because of this cascade of intramolecular events, the chromophore is exposed to distinct electrostatic surface potentials, which are likely to influence the protonation equilibria at the chromophore. We suggest a comprehensive model for the light-induced switching mechanism, connecting a cascade of structural rearrangements with different protonation states of the chromophore.

==About this Structure==

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[[Category: Single protein]]

[[Category: Trowitzsch, S.]]

[[Category: Wahl, M.C.]]

[[Category: Wahl, M C.]]

[[Category: Weber, G.]]

[[Category: luminescent protein; reversibly switchable fluorescent protein; green-fluorescent protein-like protein]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:31:49 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-Dronpa is a novel GFP-like fluorescent protein with exceptional, light-controlled switching properties. It may be reversibly switched, between a fluorescent on-state and a nonfluorescent off-state by, irradiation with light. To elucidate the molecular basis of the switching, mechanism, we generated reversibly switchable Dronpa protein crystals., Using these crystals we determined the elusive dark-state structure of, Dronpa at 1.95-A resolution. We found that the photoswitching results in a, cis-trans isomerization of the chromophore accompanied by complex, structural rearrangements of four nearby amino acid residues. Because of, this cascade of intramolecular events, the chromophore is exposed to, distinct electrostatic surface potentials, which are likely to influence, the protonation equilibria at the chromophore. We suggest a comprehensive, model for the light-induced switching mechanism, connecting a cascade of, structural rearrangements with different protonation states of the, chromophore.
+Dronpa is a novel GFP-like fluorescent protein with exceptional light-controlled switching properties. It may be reversibly switched between a fluorescent on-state and a nonfluorescent off-state by irradiation with light. To elucidate the molecular basis of the switching mechanism, we generated reversibly switchable Dronpa protein crystals. Using these crystals we determined the elusive dark-state structure of Dronpa at 1.95-A resolution. We found that the photoswitching results in a cis-trans isomerization of the chromophore accompanied by complex structural rearrangements of four nearby amino acid residues. Because of this cascade of intramolecular events, the chromophore is exposed to distinct electrostatic surface potentials, which are likely to influence the protonation equilibria at the chromophore. We suggest a comprehensive model for the light-induced switching mechanism, connecting a cascade of structural rearrangements with different protonation states of the chromophore.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Trowitzsch, S.]]
-[[Category: Wahl, M.C.]]
+[[Category: Wahl, M C.]]
 [[Category: Weber, G.]]
 [[Category: luminescent protein; reversibly switchable fluorescent protein; green-fluorescent protein-like protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:07:01 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:31:49 2008''