3hev

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{{Seed}}
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[[Image:3hev.png|left|200px]]
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[[Image:3hev.jpg|left|200px]]
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===Cyclic residues in alpha/beta-peptide helix bundles: GCN4-pLI side chain sequence on an (alpha-alpha-beta) backbone with a cyclic beta-residue at position 19===
===Cyclic residues in alpha/beta-peptide helix bundles: GCN4-pLI side chain sequence on an (alpha-alpha-beta) backbone with a cyclic beta-residue at position 19===
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The line below this paragraph, {{ABSTRACT_PUBMED_20718422}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 20718422 is the PubMed ID number.
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{{ABSTRACT_PUBMED_20718422}}
==About this Structure==
==About this Structure==
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3HEV is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HEV OCA].
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[[3hev]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HEV OCA].
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==Reference==
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<ref group="xtra">PMID:020718422</ref><references group="xtra"/>
[[Category: Gellman, S H.]]
[[Category: Gellman, S H.]]
[[Category: Horne, W S.]]
[[Category: Horne, W S.]]
[[Category: Price, J L.]]
[[Category: Price, J L.]]
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[[Category: Alpha/beta-peptide]]
 
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[[Category: Coiled coil]]
 
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[[Category: De novo protein]]
 
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[[Category: Foldamer]]
 
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[[Category: Helix bundle]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 21 10:53:49 2010''
 

Revision as of 05:45, 18 May 2011

Template:STRUCTURE 3hev

Cyclic residues in alpha/beta-peptide helix bundles: GCN4-pLI side chain sequence on an (alpha-alpha-beta) backbone with a cyclic beta-residue at position 19

Template:ABSTRACT PUBMED 20718422

About this Structure

3hev is a 1 chain structure. Full crystallographic information is available from OCA.

Reference

  • Price JL, Horne WS, Gellman SH. Structural consequences of beta-amino acid preorganization in a self-assembling alpha/beta-peptide: fundamental studies of foldameric helix bundles. J Am Chem Soc. 2010 Sep 8;132(35):12378-87. PMID:20718422 doi:10.1021/ja103543s

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