Insights into the Molecular Architecture of a Peptide Nanotube Using FTIR and Solid-State NMR Spectroscopic Measurements on an Aligned Sample
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...
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| Veröffentlicht in: | Angewandte Chemie International Edition 2013-09, Vol.52 (40), p.10537-10540 |
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| container_issue | 40 |
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| container_title | Angewandte Chemie International Edition |
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| creator | Middleton, David A. Madine, Jillian Castelletto, Valeria Hamley, Ian W. |
| description | 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. |
| doi_str_mv | 10.1002/anie.201301960 |
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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.</description><edition>International ed. in English</edition><identifier>ISSN: 1433-7851</identifier><identifier>EISSN: 1521-3773</identifier><identifier>DOI: 10.1002/anie.201301960</identifier><identifier>PMID: 23955926</identifier><identifier>CODEN: ACIEAY</identifier><language>eng</language><publisher>Weinheim: WILEY-VCH Verlag</publisher><subject>Alignment ; Architecture ; Communications ; Diffraction ; Helical ; IR spectroscopy ; Molecular Structure ; Nanostructure ; nanotubes ; Nanotubes, Peptide - chemistry ; NMR spectroscopy ; Nuclear magnetic resonance ; Nuclear Magnetic Resonance, Biomolecular - instrumentation ; Nuclear Magnetic Resonance, Biomolecular - methods ; Oligopeptides - chemistry ; Peptides ; Spectroscopy ; Spectroscopy, Fourier Transform Infrared - instrumentation ; Spectroscopy, Fourier Transform Infrared - methods</subject><ispartof>Angewandte Chemie International Edition, 2013-09, Vol.52 (40), p.10537-10540</ispartof><rights>2013 The Authors. Published by Wiley‐VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.</rights><rights>Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.</rights><rights>2013 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.</rights><rights>2013 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. 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Chem. Int. Ed</addtitle><description>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. 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Chem. Int. Ed</addtitle><date>2013-09-27</date><risdate>2013</risdate><volume>52</volume><issue>40</issue><spage>10537</spage><epage>10540</epage><pages>10537-10540</pages><issn>1433-7851</issn><eissn>1521-3773</eissn><coden>ACIEAY</coden><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 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.</abstract><cop>Weinheim</cop><pub>WILEY-VCH Verlag</pub><pmid>23955926</pmid><doi>10.1002/anie.201301960</doi><tpages>4</tpages><edition>International ed. in English</edition><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Alignment Architecture Communications Diffraction Helical IR spectroscopy Molecular Structure Nanostructure nanotubes Nanotubes, Peptide - chemistry NMR spectroscopy Nuclear magnetic resonance Nuclear Magnetic Resonance, Biomolecular - instrumentation Nuclear Magnetic Resonance, Biomolecular - methods Oligopeptides - chemistry Peptides Spectroscopy Spectroscopy, Fourier Transform Infrared - instrumentation Spectroscopy, Fourier Transform Infrared - methods |
| title | 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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