4c3c: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4c3c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thaumatococcus_daniellii Thaumatococcus daniellii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C3C FirstGlance]. <br> | <table><tr><td colspan='2'>[[4c3c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thaumatococcus_daniellii Thaumatococcus daniellii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C3C FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4c3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3c OCA], [https://pdbe.org/4c3c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c3c RCSB], [https://www.ebi.ac.uk/pdbsum/4c3c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c3c ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4c3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3c OCA], [https://pdbe.org/4c3c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c3c RCSB], [https://www.ebi.ac.uk/pdbsum/4c3c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c3c ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/THM1_THADA THM1_THADA] Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We describe a method for performing time-resolved X-ray crystallographic experiments based on the Hadamard transform, in which time resolution is defined by the underlying periodicity of the probe pulse sequence, and signal/noise is greatly improved over that for the fastest pump-probe experiments depending on a single pulse. This approach should be applicable on standard synchrotron beamlines and will enable high-resolution measurements of protein and small-molecule structural dynamics. It is also applicable to other time-resolved measurements where a probe can be encoded, such as pump-probe spectroscopy. | |||
Time-resolved crystallography using the Hadamard transform.,Yorke BA, Beddard GS, Owen RL, Pearson AR Nat Methods. 2014 Nov;11(11):1131-4. doi: 10.1038/nmeth.3139. Epub 2014 Oct 5. PMID:25282611<ref>PMID:25282611</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4c3c" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 15:02, 20 December 2023
Thaumatin refined against hatrx data for time-point 1Thaumatin refined against hatrx data for time-point 1
Structural highlights
FunctionTHM1_THADA Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis. Publication Abstract from PubMedWe describe a method for performing time-resolved X-ray crystallographic experiments based on the Hadamard transform, in which time resolution is defined by the underlying periodicity of the probe pulse sequence, and signal/noise is greatly improved over that for the fastest pump-probe experiments depending on a single pulse. This approach should be applicable on standard synchrotron beamlines and will enable high-resolution measurements of protein and small-molecule structural dynamics. It is also applicable to other time-resolved measurements where a probe can be encoded, such as pump-probe spectroscopy. Time-resolved crystallography using the Hadamard transform.,Yorke BA, Beddard GS, Owen RL, Pearson AR Nat Methods. 2014 Nov;11(11):1131-4. doi: 10.1038/nmeth.3139. Epub 2014 Oct 5. PMID:25282611[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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