title: Tandem Incorporation of Enantiomeric Residues Engenders Discrete Peptoid Structures.
abstract: A new peptoid design strategy entailing the concurrent inclusion of enantiomeric side chains enabled the construction of several new structural motifs, including a newly characterized "ω-strand". This new architectural technique significantly expands peptoid structural and functional space and can potentially be applied to other foldameric systems.
authors.affiliation: Department of Chemistry, Bowdoin College , 6600 College Station, Brunswick, Maine 04011-8466, United States.
authors.forename: Benjamin C
authors.initials: BC
authors.lastname: Gorske
authors.affiliation: Department of Chemistry, Bowdoin College , 6600 College Station, Brunswick, Maine 04011-8466, United States.
authors.forename: Emily M
authors.initials: EM
authors.lastname: Mumford
authors.affiliation: Department of Chemistry, Colby College , 5750 Mayflower Hill, Waterville, Maine 04901, United States.
authors.forename: Rebecca R
authors.initials: RR
authors.lastname: Conry