Curtis-Marof, Rose, Doko, Denisa, Rowe, Michelle L., Richards, Kirsty L., Williamson, Richard A., Howard, Mark J. (2014) 19F NMR spectroscopy monitors ligand binding to recombinantly fluorine-labelled b?x from human protein disulphide isomerase (hPDI). Organic & Biomolecular Chemistry, 12 (23). pp. 3808-3812. ISSN 1477-0520. (doi:10.1039/c4ob00699b) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:41110)
| The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. | |
| Official URL: http://dx.doi.org/10.1039/c4ob00699b |
Abstract
We report a protein-observe 19F NMR-based ligand titration binding study of human PDI b?x with ?-somatostatin that also emphasises the need to optimise recombinant protein fluorination when using 5- or 6-fluoroindole. This study highlights a recombinant preference for 5-fluoroindole over 6-fluoroindole; most likely due to the influence of fluorine atomic packing within the folded protein structure. Fluorination affords a single 19F resonance probe to follow displacement of the protein x-linker as ligand is titrated and provides a dissociation constant of 23 ± 4 ?M.
| Item Type: | Article |
|---|---|
| DOI/Identification number: | 10.1039/c4ob00699b |
| Subjects: | Q Science |
| Divisions: | Divisions > Division of Natural Sciences > Biosciences |
| Depositing User: | Susan Davies |
| Date Deposited: | 21 May 2014 13:27 UTC |
| Last Modified: | 17 Aug 2022 10:57 UTC |
| Resource URI: | https://kar.kent.ac.uk/id/eprint/41110 (The current URI for this page, for reference purposes) |
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