Conformation of di-n-propylglycine residues (Dpg) in peptides: crystal structures of a type I' β-turn forming tetrapeptide and an α-helical tetradecapeptide

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dc.contributor.author Hegde, RP en
dc.contributor.author Aravinda, S en
dc.contributor.author Rai, R en
dc.contributor.author Kaul, R en
dc.contributor.author Sarojini Amma, Vijayalekshmi en
dc.contributor.author Rao, RB en
dc.contributor.author Shamala, N en
dc.contributor.author Balaram, P en
dc.date.accessioned 2012-02-23T00:21:22Z en
dc.date.issued 2008 en
dc.identifier.citation Journal of Peptide Science 14(5):648-659 2008 en
dc.identifier.issn 1075-2617 en
dc.identifier.uri http://hdl.handle.net/2292/11685 en
dc.description.abstract The crystal structures of two oligopeptides containing di-n-propylglycine (Dpg) residues, Boc-Gly-Dpg-Gly-Leu-OMe (1) and Boc-Val-Ala-Leu-Dpg-Val-Ala-Leu-Val-Ala-Leu-Dpg-Val-Ala-Leu-OMe (2) are presented. Peptide 1 adopts a type I'β - turn conformation with Dpg(2)-Gly(3) at the corner positions. The 14-residue peptide 2 crystallizes with two molecules in the asymmetric unit, both of which adopt α-helical conformations stabilized by 11 successive 5 → 1 hydrogen bonds. In addition, a single 4 → 1 hydrogen bond is also observed at the N-terminus. All five Dpg residues adopt backbone torsion angles (Φ, ψ) in the helical region of conformational space. Evaluation of the available structural data on Dpg peptides confirm the correlation between backbone bond angle N-C^α - C'(τ) and the observed backbone Φ, ψ values. For τ > 106°, helices are observed, while fully extended structures are characterized by τ < 106°. The mean τ values for extended and folded conformations for the Dpg residue are 103.6° ± 1.7° and 109.9° ± 2.6°, respectively. en
dc.language English en
dc.publisher John Wiley & Sons Ltd. en
dc.relation.ispartofseries Journal of Peptide Science en
dc.rights Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. Detals obtained from: http://www.sherpa.ac.uk/romeo/issn/1075-2617/ en
dc.rights.uri https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm en
dc.title Conformation of di-n-propylglycine residues (Dpg) in peptides: crystal structures of a type I' β-turn forming tetrapeptide and an α-helical tetradecapeptide en
dc.type Journal Article en
dc.identifier.doi 10.1002/psc.962 en
pubs.issue 5 en
pubs.begin-page 648 en
pubs.volume 14 en
dc.rights.holder Copyright: John Wiley & Sons Ltd. en
pubs.end-page 659 en
dc.rights.accessrights http://purl.org/eprint/accessRights/RestrictedAccess en
pubs.subtype Article en
pubs.elements-id 79880 en
pubs.org-id Science en
pubs.org-id Chemistry en
pubs.record-created-at-source-date 2010-09-01 en


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