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1
Q45044172-A7D38D1F-E4FC-4482-B4A6-62A0F1175DA0
Q45044172-A7D38D1F-E4FC-4482-B4A6-62A0F1175DA0
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http://www.wikidata.org/entity/statement/Q45044172-A7D38D1F-E4FC-4482-B4A6-62A0F1175DA0
BeF(x) stops the chaperonin cycle of GroEL-GroES and generates a complex with double folding chambers.
P2860
Q45044172-A7D38D1F-E4FC-4482-B4A6-62A0F1175DA0
BestRank
Statement
http://www.wikidata.org/entity/statement/Q45044172-A7D38D1F-E4FC-4482-B4A6-62A0F1175DA0
rank
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type
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wasDerivedFrom
ff23c5ea169ab9c8a49b10dab36e2bc8a96aa8ca
P2860
On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES.