5bql
From Proteopedia
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<table><tr><td colspan='2'>[[5bql]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BQL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BQL FirstGlance]. <br> | <table><tr><td colspan='2'>[[5bql]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BQL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BQL FirstGlance]. <br> | ||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NRQ:{(4Z)-4-(4-HYDROXYBENZYLIDENE)-2-[3-(METHYLTHIO)PROPANIMIDOYL]-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>NRQ</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NRQ:{(4Z)-4-(4-HYDROXYBENZYLIDENE)-2-[3-(METHYLTHIO)PROPANIMIDOYL]-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>NRQ</scene></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=5bql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bql OCA], [http://pdbe.org/5bql PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bql RCSB], [http://www.ebi.ac.uk/pdbsum/5bql PDBsum]</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=5bql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bql OCA], [http://pdbe.org/5bql PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bql RCSB], [http://www.ebi.ac.uk/pdbsum/5bql PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5bql ProSAT]</span></td></tr> |
</table> | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Forster or fluorescence resonance energy transfer (FRET) technology and genetically encoded FRET biosensors provide a powerful tool for visualizing signaling molecules in live cells with high spatiotemporal resolution. Fluorescent proteins (FPs) are most commonly used as both donor and acceptor fluorophores in FRET biosensors, especially since FPs are genetically encodable and live-cell compatible. In this review, we will provide an overview of methods to measure FRET changes in biological contexts, discuss the palette of FP FRET pairs developed and their relative strengths and weaknesses, and note important factors to consider when using FPs for FRET studies. | ||
+ | |||
+ | A Guide to Fluorescent Protein FRET Pairs.,Bajar BT, Wang ES, Zhang S, Lin MZ, Chu J Sensors (Basel). 2016 Sep 14;16(9). pii: E1488. doi: 10.3390/s16091488. PMID:27649177<ref>PMID:27649177</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 5bql" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Revision as of 13:54, 5 October 2016
Fluorescent protein cyOFP
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Categories: Ataie, N | Chu, J | Lin, M Z | Ng, H L | Sens, A | Fluorescent protein