Ontology highlight
ABSTRACT:
SUBMITTER: Johnson LM
PROVIDER: S-EPMC3928965 | biostudies-literature | 2013
REPOSITORIES: biostudies-literature
Johnson Lisa M LM Gellman Samuel H SH
Methods in enzymology 20130101
We describe a general strategy for creating peptidic oligomers that have unnatural backbones but nevertheless adopt a conformation very similar to the α-helix. These oligomers contain both α- and β-amino acid residues (α/β-peptides). If the β content reaches 25-30% of the residue total, and the β residues are evenly distributed along the backbone, then substantial resistance to proteolytic degradation is often observed. These α/β-peptides can mimic the informational properties of α-helices invol ...[more]