6nqr: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6nqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nqr OCA], [http://pdbe.org/6nqr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nqr RCSB], [http://www.ebi.ac.uk/pdbsum/6nqr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nqr ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6nqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nqr OCA], [http://pdbe.org/6nqr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nqr RCSB], [http://www.ebi.ac.uk/pdbsum/6nqr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nqr ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Rotation around a specific bond after photoexcitation is central to vision and emerging opportunities in optogenetics, super-resolution microscopy, and photoactive molecular devices. Competing roles for steric and electrostatic effects that govern bond-specific photoisomerization have been widely discussed, the latter originating from chromophore charge transfer upon excitation. We systematically altered the electrostatic properties of the green fluorescent protein chromophore in a photoswitchable variant, Dronpa2, using amber suppression to introduce electron-donating and electron-withdrawing groups to the phenolate ring. Through analysis of the absorption (color), fluorescence quantum yield, and energy barriers to ground- and excited-state isomerization, we evaluate the contributions of sterics and electrostatics quantitatively and demonstrate how electrostatic effects bias the pathway of chromophore photoisomerization, leading to a generalized framework to guide protein design. | |||
Electrostatic control of photoisomerization pathways in proteins.,Romei MG, Lin CY, Mathews II, Boxer SG Science. 2020 Jan 3;367(6473):76-79. doi: 10.1126/science.aax1898. PMID:31896714<ref>PMID:31896714</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6nqr" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Dronpa|Dronpa]] | *[[Dronpa|Dronpa]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 12:01, 5 February 2020
Crystal structure of fast switching M159T mutant of fluorescent protein Dronpa (Dronpa2)- Y63(3-NO2Y)Crystal structure of fast switching M159T mutant of fluorescent protein Dronpa (Dronpa2)- Y63(3-NO2Y)
Structural highlights
Publication Abstract from PubMedRotation around a specific bond after photoexcitation is central to vision and emerging opportunities in optogenetics, super-resolution microscopy, and photoactive molecular devices. Competing roles for steric and electrostatic effects that govern bond-specific photoisomerization have been widely discussed, the latter originating from chromophore charge transfer upon excitation. We systematically altered the electrostatic properties of the green fluorescent protein chromophore in a photoswitchable variant, Dronpa2, using amber suppression to introduce electron-donating and electron-withdrawing groups to the phenolate ring. Through analysis of the absorption (color), fluorescence quantum yield, and energy barriers to ground- and excited-state isomerization, we evaluate the contributions of sterics and electrostatics quantitatively and demonstrate how electrostatic effects bias the pathway of chromophore photoisomerization, leading to a generalized framework to guide protein design. Electrostatic control of photoisomerization pathways in proteins.,Romei MG, Lin CY, Mathews II, Boxer SG Science. 2020 Jan 3;367(6473):76-79. doi: 10.1126/science.aax1898. PMID:31896714[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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