Journal of the American Chemical Society · 2003 · 106 citations · 18 references
Life SciencesBiochemistryBiophysicsProtein FoldingStructural BiochemistryStructural BiologyMacromolecular AssemblyPeptide ChemistryProtein OligomerizationProtein StructureSecondary StructureSecondary Structure FormationChiralityChirality Of Amino AcidsPeptide Bond GeometryPeptide Structure Analysis
The C-linked carbo-beta-peptides, oligomers of a new class of C-linked carbo-beta3-amino acids, have been shown to generate mixed 12/10 and 10/12 helices. The design involves use of "alternating chirality" of the epimeric (at the amine center) monomers to control the stability of these helices. The observation of stable 12/10 helix in a tripeptide and 10/12 helix in a tetrapeptide is unprecedented.
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Samuel H. Gellman · Accounts of Chemical Research · 1998 · 2.5K citations
β-Peptides: a surprise at every turn
Dieter Seebàch, J. L. Matthews · Chemical Communications · 1997 · 775 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