Wagstaff, Jane L., Vallath, Sabari, Marshall, John F., Williamson, Richard A., Howard, Mark J. (2010) Two-dimensional heteronuclear saturation transfer difference NMR reveals detailed integrin alphavbeta6 protein-peptide interactions. Chemical Communications, 46 (40). pp. 7533-7535. ISSN 1359-7345. (doi:10.1039/c0cc01846e) (Access to this publication is currently restricted. You may be able to access a copy if URLs are provided) (KAR id:28016)
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Official URL: http://dx.doi.org/10.1039/c0cc01846e |
Abstract
We report the first example of peptide-protein heteronuclear two-dimensional (2D) saturation transfer difference nuclear magnetic resonance (STD NMR). This method, resulting in dramatically reduced overlap, was applied to the interaction of the integrin alphavbeta6 with a known peptide ligand and highlights novel contact points between the substrate and target protein.
Item Type: | Article |
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DOI/Identification number: | 10.1039/c0cc01846e |
Additional information: | Wagstaff, Jane L Vallath, Sabari Marshall, John F Williamson, Richard A Howard, Mark J England Chemical communications (Cambridge, England) Chem Commun (Camb). 2010 Oct 28;46(40):7533-5. Epub 2010 Sep 13. |
Uncontrolled keywords: | Amino Acid Sequence Antigens, Neoplasm/chemistry/*metabolism Binding Sites Foot-and-Mouth Disease Virus/chemistry/*metabolism Humans Integrins/chemistry/*metabolism Models, Molecular Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular/*methods Peptides/chemistry/*metabolism Protein Binding Receptors, Virus/chemistry/*metabolism |
Subjects: |
Q Science > QD Chemistry Q Science > QH Natural history > QH301 Biology T Technology > TP Chemical technology |
Divisions: | Divisions > Division of Natural Sciences > Biosciences |
Depositing User: | M.J. Howard |
Date Deposited: | 15 Jul 2011 14:42 UTC |
Last Modified: | 05 Nov 2024 10:09 UTC |
Resource URI: | https://kar.kent.ac.uk/id/eprint/28016 (The current URI for this page, for reference purposes) |
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