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- W2951777218 abstract "Unlike α-amino acids, peptides formed from β-amino acids (β-peptides) display stability toward enzymatic degradation and may form turns and helices with as few as four residues. Because both the Cα and Cβ of the β-amino acid may bear substituents, a large number of β-amino acids can be synthesized. β-Peptides form various well-defined secondary structures, including 14-helix, 12-helix, 10/12-helix, 10-helix, 8-helix, turn structures, sheets, and hairpins. For all of these reasons, β-amino acids have been increasingly used as building blocks for molecular design and pharmaceutical applications. To explain the conformational features of β-peptides, several quantum mechanics and molecular dynamics studies that rationalize the observed conformational features have been reported. However, a systematic account that unifies various factors critical to the conformational features is still lacking. In this Account, we present a detailed analysis of the conformational features of various β-peptides. We start by stu..." @default.
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- W2951777218 date "2009-01-13" @default.
- W2951777218 modified "2023-10-11" @default.
- W2951777218 title "ChemInform Abstract: Theoretical Analysis of Secondary Structures of β-Peptides" @default.
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- W2951777218 doi "https://doi.org/10.1002/chin.200902275" @default.
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