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7tmh
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 7tmh is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Porous framework formed by assembly of a bipyridyl-conjugated helical peptide== | |
| + | <StructureSection load='7tmh' size='340' side='right'caption='[[7tmh]], [[Resolution|resolution]] 0.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7tmh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TMH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TMH FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.8Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AIB:ALPHA-AMINOISOBUTYRIC+ACID'>AIB</scene>, <scene name='pdbligand=CCN:ACETONITRILE'>CCN</scene>, <scene name='pdbligand=I6W:ethyl+5-formyl[2,2-bipyridine]-5-carboxylate'>I6W</scene>, <scene name='pdbligand=I77:5-(hydrazinecarbonyl)[2,2-bipyridine]-5-carboxamide'>I77</scene>, <scene name='pdbligand=PHI:IODO-PHENYLALANINE'>PHI</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=7tmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tmh OCA], [https://pdbe.org/7tmh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tmh RCSB], [https://www.ebi.ac.uk/pdbsum/7tmh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tmh ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The evolution of proteins from simpler, self-assembled peptides provides a powerful blueprint for the design of complex synthetic materials. Previously, peptide-metal frameworks using short sequences (</=3 residues) have shown great promise as proteomimetic materials that exhibit sophisticated capabilities. However, their development has been hindered due to few variable residues and restricted choice of side-chains that are compatible with metal ions. Herein, we developed a noncovalent strategy featuring pi-stacking bipyridyl residues to assemble much longer peptides into crystalline frameworks that tolerate even previously incompatible acidic and basic functionalities and allow an unprecedented level of pore variations. Single-crystal X-ray structures are provided for all variants to guide and validate rational design. These materials exhibit hallmark proteomimetic behaviors such as guest-selective induced fit and assembly of multimetallic units. Significantly, we demonstrate facile optimization of the framework design to substantially increase affinity toward a complex organic molecule. | ||
| - | + | Assembly of pi-Stacking Helical Peptides into a Porous and Multivariable Proteomimetic Framework.,Heinz-Kunert SL, Pandya A, Dang VT, Tran PN, Ghosh S, McElheny D, Santarsiero BD, Ren Z, Nguyen AI J Am Chem Soc. 2022 Apr 20;144(15):7001-7009. doi: 10.1021/jacs.2c02146. Epub, 2022 Apr 7. PMID:35390261<ref>PMID:35390261</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7tmh" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Nguyen AI]] | ||
Current revision
Porous framework formed by assembly of a bipyridyl-conjugated helical peptide
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