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

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
, Will Dawson
, Matthew P Crump
, Rudolf K Allemann

Research output: Contribution to journal › Article (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 language	English
Pages (from-to)	61-64
Journal	Biomolecular NMR Assignments
Volume	7
DOIs	https://doi.org/10.1007/s12104-012-9378-x
Publication status	Published - 2013

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Loveridge, E. J., Matthews, S. M., Williams, C., Whittaker, S. B.-M., Günther, U. L., Evans, R. M., Dawson, W., Crump, M. P., & Allemann, R. K. (2013). 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, 7, 61-64. https://doi.org/10.1007/s12104-012-9378-x

@article{13044ca13ad84e77a09f66337d0c3465,

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 Will Dawson and Crump, \{Matthew P\} and Allemann, \{Rudolf K\}",

year = "2013",

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

language = "English",

volume = "7",

pages = "61--64",

journal = "Biomolecular NMR Assignments",

issn = "1874-270X",

publisher = "Springer Science and Business Media B.V.",

}

Loveridge, EJ, Matthews, SM, Williams, C, Whittaker, SB-M, Günther, UL, Evans, RM, Dawson, W, Crump, MP & Allemann, RK 2013, '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, vol. 7, pp. 61-64. https://doi.org/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. / Loveridge, E Joel; Matthews, Stella M; Williams, Christopher et al.
In: Biomolecular NMR Assignments, Vol. 7, 2013, p. 61-64.

Research output: Contribution to journal › Article (Academic Journal) › peer-review

TY - JOUR

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, Will

AU - Crump, Matthew P

AU - Allemann, Rudolf K

PY - 2013

Y1 - 2013

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 (Academic Journal)

C2 - 22415546

SN - 1874-270X

VL - 7

SP - 61

EP - 64

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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