title: Insights into the molecular architecture of a peptide nanotube using FTIR and solid-state NMR spectroscopic measurements on an aligned sample.
abstract: 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 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.
authors: Institute of Integrative Biology, University of Liverpool, Crown Street, Liverpool L69 7ZB (UK). middleda@liverpool.ac.uk.
authors: David A
authors: DA
authors: Middleton
authors: Jillian
authors: J
authors: Madine
authors: Valeria
authors: V
authors: Castelletto
authors: Ian W
authors: IW
authors: Hamley
mesh_terms: D015394:Molecular Structure; D045333:Nanotubes, Peptide / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000295:instrumentation / Q000379:methods; D009842:Oligopeptides / Q000737:chemistry; D017550:Spectroscopy, Fourier Transform Infrared / Q000295:instrumentation / Q000379:methods
chemical_list: D045333:Nanotubes, Peptide; D009842:Oligopeptides
keywords: IR spectroscopy; NMR spectroscopy; nanotubes; peptides
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