View source for 7tmj


==Porous framework formed by assembly of a bipyridyl-conjugated helical peptide==
<StructureSection load='7tmj' size='340' side='right'caption='[[7tmj]], [[Resolution|resolution]] 1.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TMJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TMJ 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]] 1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AG:SILVER+ION'>AG</scene>, <scene name='pdbligand=AIB:ALPHA-AMINOISOBUTYRIC+ACID'>AIB</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=NO3:NITRATE+ION'>NO3</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=7tmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tmj OCA], [https://pdbe.org/7tmj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tmj RCSB], [https://www.ebi.ac.uk/pdbsum/7tmj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tmj ProSAT]</span></td></tr>
</table>
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== 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 (&lt;/=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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7tmj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Nguyen AI]]