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Ab initio:
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Fragment-based:
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Structure from chemical shifts:
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Disordered proteins:
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From NMR-STAR 3.1
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NMR sample preparation:
Protein disorder:
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Protein solubility:
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Solid-state NMR:
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Default 1H NMR studies on the oxidized ferredoxin from Clostridium pasteurianum.

1H NMR studies on the oxidized ferredoxin from Clostridium pasteurianum.

Related Articles 1H NMR studies on the oxidized ferredoxin from Clostridium pasteurianum.

Biochem Int. 1992 Mar;26(4):577-85

Authors: Ganadu ML, Bonomi F, Pagani S, Boelens R

The 8Fe-8S ferredoxin from Clostridium pasteurianum was investigated by 1D and 2D 1H NMR. Spectra of a well-structured, full native preparation of the oxidized protein in 1 M NaCl at pH 8.0 are presented. Assignments of non-isotropically shifted resonances in the diamagnetic region of the spectrum, namely those of the unique aromatic residues F30 and Y2, are presented for the first time.

PMID: 1610368 [PubMed - indexed for MEDLINE]



Source: PubMed
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