Literature DB >> 15214438

A study of a Calpha,beta-didehydroalanine homo-oligopeptide series in the solid-state by 13C cross-polarization magic angle spinning NMR.

Katherine A Henzler Wildman1, Ayyalusamy Ramamoorthy, Tateaki Wakamiya, Taichi Yoshikawa, Marco Crisma, Claudio Toniolo, Fernando Formaggio.   

Abstract

The fully extended peptide conformation (2.0(5)-helix) has been investigated for the first time in the solid-state by 13C cross-polarization magic angle spinning NMR. The compounds examined are members of a terminally protected, homo-oligopeptide series (from monomer through hexamer) based on Calpha,beta-didehydroalanine.

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Year:  2004        PMID: 15214438     DOI: 10.1002/psc.551

Source DB:  PubMed          Journal:  J Pept Sci        ISSN: 1075-2617            Impact factor:   1.905


  1 in total

1.  Conformation of dehydropentapeptides containing four achiral amino acid residues - controlling the role of L-valine.

Authors:  Michał Jewgiński; Joanna Krzciuk-Gula; Maciej Makowski; Rafał Latajka; Paweł Kafarski
Journal:  Beilstein J Org Chem       Date:  2014-03-14       Impact factor: 2.883

  1 in total

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