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NMR characterization of the NADP(H)-binding domain of Escherichia coli transhydrogenase: sequential assignment and global fold

✍ Scribed by Carina Johansson; Anders Bergkvist; Ola Fjellström; Jan Rydström; B.Göran Karlsson


Book ID
117111411
Publisher
Elsevier Science
Year
1999
Tongue
English
Weight
248 KB
Volume
458
Category
Article
ISSN
0014-5793

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The oxidized form of the mercuric ion binding protein MerP has been studied by two-dimensional NMR. MerP, which is a periplasmic water-soluble protein with 72 amino acids, is involved in the detoxification of mercuric ions in bacteria with resistance against mercury. The mercuric ions in the peripla