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Helix Formation in Preorganized β/γ-Peptide Foldamers: Hydrogen-Bond Analogy to the α-Helix without α-Amino Acid Residues
We report the first high-resolution structural data for the β/γ-peptide 13-helix (i,i+3 C=O···H-N H-bonds), a secondary structure that is formed by oligomers with a 1:1 alternation of β- and γ-amino acid residues. Our characterization includes both crystallophaphic and 2D NMR data. Previous studies...
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| Main Authors: | , , , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
2010
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2904518/ https://ncbi.nlm.nih.gov/pubmed/20491510 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/ja103233a |
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