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Q28486787-CFE3F59D-ADD8-4320-B6CE-D7A6503C4B8A
Q28486787-CFE3F59D-ADD8-4320-B6CE-D7A6503C4B8A
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http://www.wikidata.org/entity/statement/Q28486787-CFE3F59D-ADD8-4320-B6CE-D7A6503C4B8A
The Mycobacterium tuberculosis small heat shock protein Hsp16.3 exposes hydrophobic surfaces at mild conditions: conformational flexibility and molecular chaperone activity
P2860
Q28486787-CFE3F59D-ADD8-4320-B6CE-D7A6503C4B8A
BestRank
Statement
http://www.wikidata.org/entity/statement/Q28486787-CFE3F59D-ADD8-4320-B6CE-D7A6503C4B8A
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wasDerivedFrom
e8f30ba7459db34f22eb9583f29ef534dee81228
P2860
The guanidine-induced conformational changes of the chaperonin GroEL from Escherichia coli. Evidence for the existence of an unfolding intermediate state.