Issue 18, 2013
From the journal:

Chemical Communications

Measuring proteinreduction potentials using 15N HSQCNMR spectroscopy†

Samantha L. Taylor,a   Harriet Crawley-Snowdon,a   Jane L. Wagstaff,a   Michelle L. Rowe,a   Mark Shepherd,a   Richard A. Williamson*a  and  Mark J. Howard*a  

* Corresponding authors

a School of Bioscience, University of Kent, Canterbury, Kent, UK
E-mail: r.a.williamson@kent.ac.uk, m.j.howard@kent.ac.uk
Fax: +44 (0)1227 763912
Tel: +44 (0)1227 764000

Abstract

NMR spectroscopy was used to measure reduction potentials of four redox proteins by following multiple 15N HSQC protein resonances across a titration series using mixtures of oxidised and reduced glutathione. Results for PDI a, PDI ab and DsbA agree with the literature and our result for ERp18 confirms this protein as an oxidoreductase of comparable or greater reducing strength than PDI a.

Graphical abstract: Measuring protein reduction potentials using 15N HSQC NMR spectroscopy

About
Cited by
Related
Download options Please wait...

Supplementary files

Article information

DOI
https://doi.org/10.1039/C3CC38952A
Article type
Communication
Submitted
14 Dec 2012
Accepted
22 Jan 2013
First published
22 Jan 2013
This article is Open Access
Creative Commons BY license

Chem. Commun., 2013,49, 1847-1849

Permissions

Request permissions

Measuring protein reduction potentials using 15N HSQC NMR spectroscopy

S. L. Taylor, H. Crawley-Snowdon, J. L. Wagstaff, M. L. Rowe, M. Shepherd, R. A. Williamson and M. J. Howard, Chem. Commun., 2013, 49, 1847 DOI: 10.1039/C3CC38952A

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements