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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

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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. / Middleton, David A; Madine, Jillian; Castelletto, Valeria et al.
In: Angewandte Chemie International Edition, Vol. 52, No. 40, 27.09.2013, p. 10537-10540.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

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Middleton DA, Madine J, Castelletto V, Hamley IW. Insights into the Molecular Architecture of a Peptide Nanotube Using FTIR and Solid-State NMR Spectroscopic Measurements on an Aligned Sample. Angewandte Chemie International Edition. 2013 Sept 27;52(40):10537-10540. Epub 2013 Aug 16. doi: 10.1002/anie.201301960

Author

Middleton, David A ; Madine, Jillian ; Castelletto, Valeria et al. / Insights into the Molecular Architecture of a Peptide Nanotube Using FTIR and Solid-State NMR Spectroscopic Measurements on an Aligned Sample. In: Angewandte Chemie International Edition. 2013 ; Vol. 52, No. 40. pp. 10537-10540.

Bibtex

@article{bc3f179aed7d4beb95b852c0c2b4bc44,
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.",
author = "Middleton, {David A} and Jillian Madine and Valeria Castelletto and Hamley, {Ian W}",
note = "Copyright {\textcopyright} 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.",
year = "2013",
month = sep,
day = "27",
doi = "10.1002/anie.201301960",
language = "English",
volume = "52",
pages = "10537--10540",
journal = "Angewandte Chemie International Edition",
issn = "1433-7851",
publisher = "Wiley-VCH Verlag",
number = "40",

}

RIS

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 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.

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 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.

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 -