A Peptoid Ribbon Secondary Structure1. Issue 19 (9th April 2013)

• Record Type: Journal Article
• Authors: Crapster, J. Aaron; Guzei, Ilia A.; Blackwell, Helen E.
• Is Part Of: Angewandte Chemie international edition. Volume 52:Issue 19(2013)
• Page Start: 5079
• Page End: 5084
• Publication Date: 2013-04-09
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201208630
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>Joining the fold</bold>: A series of peptoids, or oligomers of <italic>N</italic>‐substituted glycines, adopt a novel secondary structure, designated the "peptoid ribbon". This fold was stable at short chain lengths and in a variety of solvents (both organic and aqueous), and arose from a primary sequence of peptoid monomers designed to enforce an alternating pattern of <italic>cis</italic> and <italic>trans</italic> main‐chain amides.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg1zsxjg9h" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>