1H,
13C and
15N resonance assignments for the oxidized and reduced states of the N-terminal domain of DsbD from Escherichia coli

1H, 13C and 15N resonance assignments for the oxidized and reduced states of the N-terminal domain of DsbD from Escherichia coli

Pokaži ostale verzije (1)

Viability and pathogenicity of Gram-negative bacteria is linked to the cytochrome c maturation and the oxidative protein folding systems in the periplasm. The transmembrane reductant conductor DsbD is a unique protein which provides the necessary reducing power to both systems through thiol-disulfid...

Bibliografski detalji
Glavni autori:	Mavridou, D, Stelzl, L, Ferguson, S, Redfield, C
Format:	Journal article
Jezik:	English
Izdano:	Springer Netherlands 2011

Slični predmeti

1H, 13C and 15N resonance assignments for the oxidized and reduced states of the N-terminal domain of DsbD from Escherichia coli.
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1H, 15N and 13C assignments of the carboxy-terminal domain of the transmembrane electron transfer protein DsbD [2]
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Active-site properties of the oxidized and reduced C-terminal domain of DsbD obtained by NMR spectroscopy.
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Active-site properties of the oxidized and reduced C-terminal domain of DsbD obtained by NMR spectroscopy
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