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1pbz
From Proteopedia
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| - | [[ | + | ==DE NOVO DESIGNED PEPTIDE-METALLOPORPHYRIN COMPLEX, SOLUTION STRUCTURE== |
| + | <StructureSection load='1pbz' size='340' side='right' caption='[[1pbz]], [[NMR_Ensembles_of_Models | 14 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1pbz]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PBZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PBZ FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PC3:COPROPORPHYRIN+I+CONTAINING+CO(III)'>PC3</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pbz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pbz RCSB], [http://www.ebi.ac.uk/pdbsum/1pbz PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The structural characterization of de novo designed metalloproteins together with determination of chemical reactivity can provide a detailed understanding of the relationship between protein structure and functional properties. Toward this goal, we have prepared a series of cyclic peptides that bind to water-soluble metalloporphyrins (FeIII and CoIII). Neutral and positively charged histidine-containing peptides bind with a high affinity, whereas anionic peptides bind only weakly to the negatively charged metalloporphyrin. Additionally, it was found that the peptide becomes helical only in the presence of the metalloporphyrin. CD experiments confirm that the metalloporphyrin binds specific cyclic peptides with high affinity and with isodichroic behavior. Thermal unfolding experiments show that the complex has "native-like" properties. Finally, NMR spectroscopy produced well dispersed spectra and experimental restraints that provide a high-resolution solution structure of the complexed peptide. | ||
| - | + | De novo designed cyclic-peptide heme complexes.,Rosenblatt MM, Wang J, Suslick KS Proc Natl Acad Sci U S A. 2003 Nov 11;100(23):13140-5. Epub 2003 Oct 31. PMID:14595023<ref>PMID:14595023</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Rosenblatt, M M.]] | [[Category: Rosenblatt, M M.]] | ||
[[Category: Suslick, K S.]] | [[Category: Suslick, K S.]] | ||
Revision as of 06:51, 9 June 2014
DE NOVO DESIGNED PEPTIDE-METALLOPORPHYRIN COMPLEX, SOLUTION STRUCTURE
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