Chemical Communications · 2019 · 16 citations · 40 references
Life SciencesBiochemistryProtein FoldingStructural BiochemistryStructural BiologyMacromolecular StructurePeptide ChemistryProtein StructureSecondary StructureSecondary Structure FormationBeta SheetsPeptide Bond GeometryProtein Backbone Hydrogen BondsProtein Topology Formation
Enantiodiscriminative helix formation was observed for β-peptide H14 helices. This observation is caused by the synperiplanar orientation of H-O atoms which is more unfavorable than those for H-H interaction. The 1,2 H-O interaction leads to the destruction of the helical structure. The introduction of a double C-C bond in the backbone rules out helix formation.
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Samuel H. Gellman · Accounts of Chemical Research · 1998 · 2.5K citations
Dieter Seebàch, Mark Overhand, Florian N. M. Kühnle et al. · Helvetica Chimica Acta · 1996 · 719 citations
Residue-based control of helix shape in β-peptide oligomers
Daniel H. Appella, Laurie A. Christianson, Daniel A. Klein et al. · Nature · 1997 · 622 citations