Publication | Closed Access
Two Helical Conformations from a Single Foldamer Backbone: “Split Personality” in Short α/β‐Peptides
211
Citations
31
References
2004
Year
Supramolecular AssemblyProtein AssemblyShort α/β‐PeptidesMolecular BiologyPeptide ScienceAnalytical UltracentrifugationHelical Secondary StructureProtein FoldingSingle Foldamer BackboneNew FoldamersBiophysicsHelical ConformationsMonomer TypeBiochemistryConformational StudyStructural BiologyNatural SciencesPeptide SynthesisMedicine
Oligopeptides with heterogeneous backbones, i.e., oligopeptides containing more than one monomer type, may be a fruitful source of new foldamers. This conclusion was suggested by studies on oligomers comprising L-α-amino acid and cyclic β-amino acid residues in a sequentially alternating pattern, which are shown to display helical secondary structure in solution. Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2002/2004/z52125_s.pdf 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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