@article{Araghi2010betag-9806,
  year={2010},
  doi={10.1002/cbic.200900700},
  title={A beta/gamma Motif to Mimic alpha-Helical Turns in Proteins},
  number={3},
  volume={11},
  issn={1439-4227},
  journal={ChemBioChem},
  pages={335--339},
  author={Araghi, Raheleh Rezaei and Jäckel, Christian and Cölfen, Helmut and Salwiczek, Mario and Völkel, Antje and Wagner, Sara C. and Wieczorek, Sebastian and Baldauf, Carsten and Koksch, Beate}
}

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    <dcterms:bibliographicCitation>First publ. in: ChemBioChem 11 (2010), 3, pp. 335-339</dcterms:bibliographicCitation>
    <dc:creator>Araghi, Raheleh Rezaei</dc:creator>
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    <dc:contributor>Salwiczek, Mario</dc:contributor>
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    <dcterms:abstract xml:lang="eng">The combination of the properties of β- and γ-amino acids produce extended artificial fragments that recreate the properties of a natural α-helix. The substitution of two α-helical turns in an otherwise natural coiled-coil motif by a fragment of alternating β and γ-amino acids with retention of global conformation and stability of the fold was established. The new chimeric system shows a high potency in helical quaternary structure formation.</dcterms:abstract>
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    <dc:contributor>Wagner, Sara C.</dc:contributor>
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    <dc:contributor>Koksch, Beate</dc:contributor>
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    <dc:creator>Völkel, Antje</dc:creator>
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    <dc:creator>Wagner, Sara C.</dc:creator>
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