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• W2116731024 endingPage "1979" @default.
• W2116731024 startingPage "1966" @default.
• W2116731024 abstract "β-Peptides possess the ability to fold into secondary structure elements, and this property, together with resistance to biodegradation, makes these compounds interesting for pharmaceutical applications. Recently, a novel class of β-peptides containing methylidene moieties was described. The GROMOS 53A6 force field was used to simulate the folding equilibrium of a β3-hexapeptide with methylidene (CH2) groups at all six CA-atoms. Due to the rotational barriers induced by these methylidene groups, the helical secondary-structure elements, normally found in β3-peptides, are disfavored in this molecule. Simulations, started from fully extended and 314-helical conformations, showed that the molecule adopts a complete 28-helix for ca. 5% of the time and partial 28-helical conformations for ca. 20% of the time. Yet, as suggested by experiments, the folding equilibrium is dominated by unfolded conformations." @default.
• W2116731024 created "2016-06-24" @default.
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• W2116731024 date "2007-10-01" @default.
• W2116731024 modified "2023-10-03" @default.
• W2116731024 title "Folding–Unfolding Equilibrium of a Methylidene-Substitutedβ-Peptide" @default.
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• W2116731024 doi "https://doi.org/10.1002/hlca.200790204" @default.
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