1pbz

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(New page: 200px<br /><applet load="1pbz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pbz" /> '''DE NOVO DESIGNED PEPTIDE-METALLOPORPHYRIN CO...)
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[[Image:1pbz.gif|left|200px]]<br /><applet load="1pbz" size="350" color="white" frame="true" align="right" spinBox="true"
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'''DE NOVO DESIGNED PEPTIDE-METALLOPORPHYRIN COMPLEX, SOLUTION STRUCTURE'''<br />
'''DE NOVO DESIGNED PEPTIDE-METALLOPORPHYRIN COMPLEX, SOLUTION STRUCTURE'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1PBZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with ACE, NH2 and PC3 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PBZ OCA].
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1PBZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=ACE:'>ACE</scene>, <scene name='pdbligand=NH2:'>NH2</scene> and <scene name='pdbligand=PC3:'>PC3</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=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://ispc.weizmann.ac.il//pmbin/getpm?pmid=14595023 14595023]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Rosenblatt, M.M.]]
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[[Category: Rosenblatt, M M.]]
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[[Category: Suslick, K.S.]]
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[[Category: Suslick, K S.]]
[[Category: Wang, J.]]
[[Category: Wang, J.]]
[[Category: ACE]]
[[Category: ACE]]
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[[Category: peptide; metalloporphyrin; heme; de novo design]]
[[Category: peptide; metalloporphyrin; heme; de novo design]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:19:13 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:27:16 2008''

Revision as of 12:27, 21 February 2008


1pbz

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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

1PBZ is a Protein complex structure of sequences from [1] with , and as ligands. 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

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