1pbz
From Proteopedia
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[[Image:1pbz.gif|left|200px]] | [[Image:1pbz.gif|left|200px]] | ||
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'''DE NOVO DESIGNED PEPTIDE-METALLOPORPHYRIN COMPLEX, SOLUTION STRUCTURE''' | '''DE NOVO DESIGNED PEPTIDE-METALLOPORPHYRIN COMPLEX, SOLUTION STRUCTURE''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PBZ OCA]. | |
==Reference== | ==Reference== | ||
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:[http://www.ncbi.nlm.nih.gov/pubmed/14595023 14595023] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14595023 14595023] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Rosenblatt, M M.]] | [[Category: Rosenblatt, M M.]] | ||
[[Category: Suslick, K S.]] | [[Category: Suslick, K S.]] | ||
[[Category: Wang, J.]] | [[Category: Wang, J.]] | ||
| - | [[Category: | + | [[Category: De novo design]] |
| - | [[Category: | + | [[Category: Heme]] |
| - | [[Category: | + | [[Category: Metalloporphyrin]] |
| - | [[Category: | + | [[Category: Peptide]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:55:26 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 01:55, 3 May 2008
DE NOVO DESIGNED PEPTIDE-METALLOPORPHYRIN COMPLEX, SOLUTION STRUCTURE
Overview
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.
About this Structure
Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sat May 3 04:55:26 2008
