Angewandte Chemie International Edition · 2002 · 143 citations · 17 references
Life SciencesBiochemistryMolecular BiologyProtein FoldingStructural BiochemistryStructural BiologyMacromolecular AssemblyMacromolecular StructureProtein OligomerizationProtein StructureSecondary StructureSecondary Structure FormationAlpha HelicesAlpha-helix FormationBeta SheetsCoil-to-helix TransitionHelix-coil TransitionPeptide Secondary StructureProtein Backbone GeometryProtein Topology Formation
Rational control over helix and strand secondary structures is possible when conformationally restricted cyclic β-amino acid residues are incorporated in the β-peptides. Inversion of the relative configuration of these residues enables the preferred periodic structure to be switched from a helix to a single nonpolar strand (see picture).
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Samuel H. Gellman · Accounts of Chemical Research · 1998 · 2.5K citations
Peptide Folding: When Simulation Meets Experiment
Xavier Daura, Karl Gademann, Bernhard Jaun et al. · Angewandte Chemie International Edition · 1999 · 2K citations