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 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:	Cardiff Catalysis Institute (CCI) Chemistry
Subjects:	Q Science > QD Chemistry
Publisher:	Springer
ISSN:	1874-2718
Funders:	BBSRC
Last Modified:	09 Nov 2017 20:57
URI:	http://orca.cf.ac.uk/id/eprint/27857

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