Aliphatic 1H, 13C and 15N chemical shift assignments of dihydrofolate reductase from the psychropiezophile Moritella profunda in complex with NADP+ and folate

Loveridge, Edric Joel, Matthews, Stella M., Williams, Christopher, Whittaker, Sara B.-M., Günther, Ulrich L., Evans, Rhiannon M., Dawson, William Michael, Crump, Matthew P. and Allemann, Rudolf Konrad ORCID: https://orcid.org/0000-0002-1323-8830 2013. Aliphatic 1H, 13C and 15N chemical shift assignments of dihydrofolate reductase from the psychropiezophile Moritella profunda in complex with NADP+ and folate. Biomolecular NMR Assignments 7 (1) , pp. 61-64. 10.1007/s12104-012-9378-x

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Abstract

Dihydrofolate reductase from the deep-sea bacterium Moritella profunda (MpDHFR) has been 13C/15N isotopically labelled and purified. Here, we report the aliphatic 1H, 13C and 15N resonance assignments of MpDHFR in complex with NADP+ and folate. The spectra of MpDHFR suggest considerably greater conformational heterogeneity than is seen in the closely related DHFR from Escherichia coli

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Research Institutes & Centres > Cardiff Catalysis Institute (CCI) Schools > Chemistry
Subjects:	Q Science > QD Chemistry
Publisher:	Springer
ISSN:	1874-2718
Funders:	BBSRC
Last Modified:	06 Jun 2024 17:53
URI:	https://orca.cardiff.ac.uk/id/eprint/27857

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