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Q34529974-7B031FAD-AD87-4E52-AB3C-F9AD2AE052BC
Q34529974-7B031FAD-AD87-4E52-AB3C-F9AD2AE052BC
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http://www.wikidata.org/entity/statement/Q34529974-7B031FAD-AD87-4E52-AB3C-F9AD2AE052BC
In silico engineering of aggregation-prone recombinant proteins for substrate recognition by the chaperonin GroEL
P2860
Q34529974-7B031FAD-AD87-4E52-AB3C-F9AD2AE052BC
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Statement
http://www.wikidata.org/entity/statement/Q34529974-7B031FAD-AD87-4E52-AB3C-F9AD2AE052BC
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wasDerivedFrom
798b765f3a3e3f415f072a53a7c77f48c980d8eb
P2860
The 1.6-A crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad