Organic Letters · 2010 · 85 citations · 31 references
Life SciencesBiochemistryChemistryProtein FoldingStructural BiochemistryStructural BiologyFolding ThermodynamicsMacromolecular FoldingMacromolecular StructureProtein ConformationSecondary StructureSecondary Structure FormationAlpha-helix FormationHelical ConformationMolecular Folding TransitionsMolecular Modeling Of Amino Acid ConformationsPeptide FoldingSmall Protein Folding
The hexamer and octamer of trans-2-aminocyclobutane carboxylic acid were prepared and their conformational preferences studied experimentally and using molecular modeling. All observations suggest a marked preference for the folding of these oligomers into a well-defined 12-helical conformation, in both solution and the solid state.
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Samuel H. Gellman · Accounts of Chemical Research · 1998 · 2.5K citations
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Foldamers with Heterogeneous Backbones
W. Seth Horne, Samuel H. Gellman · Accounts of Chemical Research · 2008 · 682 citations · Full text
Non-haemolytic β-amino-acid oligomers
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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