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Insights into the Molecular Architecture of a Peptide Nanotube Using FTIR and Solid‐State NMR Spectroscopic Measurements on an Aligned Sample
Author(s) -
Middleton David A.,
Madine Jillian,
Castelletto Valeria,
Hamley Ian W.
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201301960
Subject(s) - fourier transform infrared spectroscopy , solid state nuclear magnetic resonance , sample (material) , nanotube , materials science , solid state , peptide , analytical chemistry (journal) , nanotechnology , carbon nanotube , chemistry , nuclear magnetic resonance , chemical engineering , organic chemistry , chromatography , physics , engineering
Queuing up : Molecular orientation within macroscopically aligned nanotubes of the peptide K 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.