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

E Joel Loveridge, Stella M Matthews, Christopher Williams, Sara B-M Whittaker, Ulrich L Günther, Rhiannon M Evans, Will Dawson, Matthew P Crump, Rudolf K Allemann

Research output: Contribution to journalArticle (Academic Journal)peer-review

2 Citations (Scopus)

Abstract

Dihydrofolate reductase from the deep-sea bacterium Moritella profunda (MpDHFR) has been (13)C/(15)N isotopically labelled and purified. Here, we report the aliphatic (1)H, (13)C and (15)N 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.
Original languageEnglish
Pages (from-to)61-64
JournalBiomolecular NMR Assignments
Volume7
DOIs
Publication statusPublished - 2013

Fingerprint Dive into the research topics of 'Aliphatic (1)H, (13)C and (15)N chemical shift assignments of dihydrofolate reductase from the psychropiezophile Moritella profunda in complex with NADP(+) and folate'. Together they form a unique fingerprint.

Cite this