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; William M Dawson; Matthew P Crump; Rudolf K Allemann

doi:10.1007/s12104-012-9378-x

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, William M Dawson, Matthew P Crump, Rudolf K Allemann

Chemistry

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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 language	English
Journal	Biomolecular NMR Assignments
DOIs	https://doi.org/10.1007/s12104-012-9378-x
Publication status	Published - 2012

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Loveridge, E. J., Matthews, S. M., Williams, C., Whittaker, S. B.-M., Günther, U. L., Evans, R. M., Dawson, W. M., Crump, M. P., & Allemann, R. K. (2012). 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. Biomolecular NMR Assignments. https://doi.org/10.1007/s12104-012-9378-x

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title = "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",

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.",

author = "Loveridge, {E Joel} and Matthews, {Stella M} and Christopher Williams and Whittaker, {Sara B-M} and G{\"u}nther, {Ulrich L} and Evans, {Rhiannon M} and Dawson, {William M} and Crump, {Matthew P} and Allemann, {Rudolf K}",

year = "2012",

doi = "10.1007/s12104-012-9378-x",

language = "English",

journal = "Biomolecular NMR Assignments",

publisher = "Springer",

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T1 - 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

AU - Loveridge, E Joel

AU - Matthews, Stella M

AU - Williams, Christopher

AU - Whittaker, Sara B-M

AU - Günther, Ulrich L

AU - Evans, Rhiannon M

AU - Dawson, William M

AU - Crump, Matthew P

AU - Allemann, Rudolf K

PY - 2012

Y1 - 2012

N2 - 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.

AB - 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.

U2 - 10.1007/s12104-012-9378-x

DO - 10.1007/s12104-012-9378-x

M3 - Article

C2 - 22415546

JO - Biomolecular NMR Assignments

JF - Biomolecular NMR Assignments

ER -

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

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