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Q41846532-24333FAF-AFC2-4A93-B7EB-26F3A2D6C5DF
Q41846532-24333FAF-AFC2-4A93-B7EB-26F3A2D6C5DF
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http://www.wikidata.org/entity/statement/Q41846532-24333FAF-AFC2-4A93-B7EB-26F3A2D6C5DF
Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability.
P2860
Q41846532-24333FAF-AFC2-4A93-B7EB-26F3A2D6C5DF
BestRank
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http://www.wikidata.org/entity/statement/Q41846532-24333FAF-AFC2-4A93-B7EB-26F3A2D6C5DF
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wasDerivedFrom
a08bf6951f28d7d868334c5754bc46437ebe1e98
P2860
The redox properties of protein disulfide isomerase (DsbA) of Escherichia coli result from a tense conformation of its oxidized form.