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cis-2-Aminocyclopentanecarboxylic Acid Oligomers Adopt a Sheetlike Structure: Switch from Helix to Nonpolar Strand
142
Citations
17
References
2002
Year
Protein AssemblyMolecular BiologyPeptide ScienceAnalytical UltracentrifugationHeterocycle ChemistryPreferred Periodic StructureChemical BiologyLinear Chain CompoundProtein FoldingRelative ConfigurationMacromolecular AssembliesNonpolar StrandBiochemistryOligonucleotideRational ControlStructural BiologySheetlike StructureNatural SciencesPeptide SynthesisMedicine
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). Supporting information for this article is available on the WWW under http://www.angewandte.com or from the author. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
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