The folding propensity of α/sulfono-γ-AA peptidic foldamers with both left- and right-handedness
Controlling the helical structure of peptide foldamers requires detailed understanding of the relationship between primary and secondary structure. Here the effect of monomer stoichiometry and configuration on the helical structures of peptide nucleic acids bearing sulfono pendants is examined.
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| Autores principales: | , , , , , , , , , , |
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| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
Nature Portfolio
2021
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| Materias: | |
| Acceso en línea: | https://doaj.org/article/d9b8f9ae63dc4df88e675993e45d2ab2 |
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| Sumario: | Controlling the helical structure of peptide foldamers requires detailed understanding of the relationship between primary and secondary structure. Here the effect of monomer stoichiometry and configuration on the helical structures of peptide nucleic acids bearing sulfono pendants is examined. |
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