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

Research output: Contribution to journalArticle

Authors

  • E Joel Loveridge
  • Stella M Matthews
  • Sara B-M Whittaker
  • Rhiannon M Evans
  • William M Dawson
  • Matthew P Crump

Colleges, School and Institutes

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.

Details

Original languageEnglish
JournalBiomolecular NMR Assignments
Publication statusPublished - 2012