19F NMR spectroscopy monitors ligand binding to recombinantly fluorine-labelled b′x from human protein disulphide isomerase (hPDI)

Curtis-Marof, Rose and Doko, Denisa and Rowe, Michelle L. and Richards, Kirsty L. and Williamson, Richard A. and 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:https://doi.org/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)

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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 Δ-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 μM.

Item Type: Article
Subjects: Q Science
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Sue Davies
Date Deposited: 21 May 2014 13:27 UTC
Last Modified: 16 Jul 2014 14:56 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/41110 (The current URI for this page, for reference purposes)
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