Journal article
Measuring protein reduction potentials using N-15 HSQC NMR spectroscopy
Chemical communications (Cambridge, England), Vol.49(18), pp.1847-1849
2013
PMID: 23360928
Abstract
NMR spectroscopy was used to measure reduction potentials of four redox proteins by following multiple N-15 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 oxido-reductase of comparable or greater reducing strength than PDI a.
Details
- Title
- Measuring protein reduction potentials using N-15 HSQC NMR spectroscopy
- Authors/Creators
- Samantha L. Taylor - Univ Kent, Sch Bioscience, Canterbury CT2 7NJ, Kent, EnglandHarriet Crawley-Snowdon - Univ Kent, Sch Bioscience, Canterbury CT2 7NJ, Kent, EnglandJane L. Wagstaff - Univ Kent, Sch Bioscience, Canterbury CT2 7NJ, Kent, EnglandMichelle L. Rowe - Univ Kent, Sch Bioscience, Canterbury CT2 7NJ, Kent, EnglandMark Shepherd - Univ Kent, Sch Bioscience, Canterbury CT2 7NJ, Kent, EnglandRichard A. Williamson - Univ Kent, Sch Bioscience, Canterbury CT2 7NJ, Kent, EnglandMark J. Howard - Univ Kent, Sch Bioscience, Canterbury CT2 7NJ, Kent, England
- Publication Details
- Chemical communications (Cambridge, England), Vol.49(18), pp.1847-1849
- Publisher
- Royal Society Chemistry
- Identifiers
- 991005587768907891
- Copyright
- © 2013 Royal Society of Chemistry
- Murdoch Affiliation
- Centre for Computational and Systems Medicine
- Language
- English
- Resource Type
- Journal article
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- Citation topics
- 1 Clinical & Life Sciences
- 1.127 Molecular & Cell Biology - Pharmacology
- 1.127.973 Thiol-Disulfide Systems
- Web Of Science research areas
- Chemistry, Multidisciplinary
- ESI research areas
- Chemistry