Insights into the Molecular Architecture of a Peptide Nanotube Using FTIR and Solid‐State NMR Spectroscopic Measurements on an Aligned Sample1. Issue 40 (16th August 2013)

• Record Type: Journal Article
• Authors: Middleton, David A.; Madine, Jillian; Castelletto, Valeria; Hamley, Ian W.
• Is Part Of: Angewandte Chemie international edition. Volume 52:Issue 40(2013)
• Page Start: 10537
• Page End: 10540
• Publication Date: 2013-08-16
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201301960
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>Queuing up</bold>: Molecular orientation within macroscopically aligned nanotubes of the peptide AAAAAAK can be studied by solid‐state NMR and IR spectroscopy. Line shape analysis of the NMR spectra indicates that the peptide NH bonds are tilted 65–70° relative to the nanotube long axis. Re‐evaluation of earlier X‐ray fiber diffraction data suggests that the peptide molecules are hydrogen‐bonded in a helical arrangement along the nanotube axis.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg3h9m308c" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>