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Local orientational disorder in peptide fibrils probed by a combination of residue-specific 13C-18O labelling, polarised infrared spectroscopy and molecular combing

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Rodríguez-Pérez, J. C., Hamley, I. W. ORCID: https://orcid.org/0000-0002-4549-0926, Gras, S. L. and Squires, A. M. (2012) Local orientational disorder in peptide fibrils probed by a combination of residue-specific 13C-18O labelling, polarised infrared spectroscopy and molecular combing. Chemical Communications, 48. pp. 11835-11837. ISSN 1359-7345

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To link to this item DOI: 10.1039/C2CC35586H

Abstract/Summary

A novel combination of site-specific isotope labelling, polarised infrared spectroscopy and molecular combing reveal local orientational ordering in the fibril-forming peptide YTIAALLSPYSGGRADS. Use of 13C-18O labelled alanine residues demonstrates that the Nterminal end of the peptide is incorporated into the cross-beta structure, while the C-terminal end shows orientational disorder

Item Type:Article
Refereed:Yes
Divisions:Interdisciplinary centres and themes > Chemical Analysis Facility (CAF)
Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:30241
Publisher:The Royal Society of Chemistry
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