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NMR Solution Structure of the Oxidized Form of MerP, a Mercuric Ion Binding Protein Involved in Bacterial Mercuric Ion Resistance †,‡

✍ Scribed by Qian, Hong; Sahlman, Lena; Eriksson, Per-Olof; Hambraeus, Charlotta; Edlund, Ulf; Sethson, Ingmar

Book ID: 126978264
Publisher: American Chemical Society
Year: 1998
Tongue: English
Weight: 107 KB
Volume: 37
Category: Article
ISSN: 0006-2960
DOI: 10.1021/bi9803628

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1H NMR studies of the mercuric ion binding protein MerP: Sequential assignment, secondary structure and global fold of oxidized MerP

✍ Per-Olof Eriksson; Lena Sahlman 📂 Article 📅 1993 🏛 Springer Netherlands 🌐 English ⚖ 830 KB

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