Research output: Contribution to Journal/Magazine › Journal article › peer-review
Research output: Contribution to Journal/Magazine › Journal article › peer-review
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TY - JOUR
T1 - Insights into the Molecular Architecture of a Peptide Nanotube Using FTIR and Solid-State NMR Spectroscopic Measurements on an Aligned Sample
AU - Middleton, David A
AU - Madine, Jillian
AU - Castelletto, Valeria
AU - Hamley, Ian W
N1 - Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
PY - 2013/9/27
Y1 - 2013/9/27
N2 - Queuing up: 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 NH 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.
AB - Queuing up: 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 NH 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.
UR - http://www.scopus.com/inward/record.url?scp=84884837572&partnerID=8YFLogxK
U2 - 10.1002/anie.201301960
DO - 10.1002/anie.201301960
M3 - Journal article
C2 - 23955926
VL - 52
SP - 10537
EP - 10540
JO - Angewandte Chemie International Edition
JF - Angewandte Chemie International Edition
SN - 1433-7851
IS - 40
ER -