1H, 13C and 15N resonance assignments for the oxidized and reduced states of the N-terminal domain of DsbD from Escherichia coli
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...
मुख्य लेखकों: | Mavridou, D, Stelzl, L, Ferguson, S, Redfield, C |
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स्वरूप: | Journal article |
भाषा: | English |
प्रकाशित: |
Springer Netherlands
2011
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समान संसाधन
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1H, 13C and 15N resonance assignments for the oxidized and reduced states of the N-terminal domain of DsbD from Escherichia coli.
द्वारा: Mavridou, D, और अन्य
प्रकाशित: (2012) -
1H, 15N and 13C assignments of the carboxy-terminal domain of the transmembrane electron transfer protein DsbD.
द्वारा: Bushell, K, और अन्य
प्रकाशित: (2002) -
1H, 15N and 13C assignments of the carboxy-terminal domain of the transmembrane electron transfer protein DsbD [2]
द्वारा: Bushell, K, और अन्य
प्रकाशित: (2002) -
Active-site properties of the oxidized and reduced C-terminal domain of DsbD obtained by NMR spectroscopy.
द्वारा: Mavridou, D, और अन्य
प्रकाशित: (2007) -
Active-site properties of the oxidized and reduced C-terminal domain of DsbD obtained by NMR spectroscopy
द्वारा: Mavridou, D, और अन्य
प्रकाशित: (2008)