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Q35478487-45B455DB-B8A9-4F68-91C9-9D82DB2264E7
Q35478487-45B455DB-B8A9-4F68-91C9-9D82DB2264E7
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http://www.wikidata.org/entity/statement/Q35478487-45B455DB-B8A9-4F68-91C9-9D82DB2264E7
The deletion of several amino acid stretches of Escherichia coli alpha-hemolysin (HlyA) suggests that the channel-forming domain contains beta-strands.
P2860
Q35478487-45B455DB-B8A9-4F68-91C9-9D82DB2264E7
BestRank
Statement
http://www.wikidata.org/entity/statement/Q35478487-45B455DB-B8A9-4F68-91C9-9D82DB2264E7
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wasDerivedFrom
5747054258c82f19ea9f0e9cc5fc4b2267ad49af
P2860
An amphipathic alpha-helix including glutamates 509 and 516 is crucial for membrane translocation of adenylate cyclase toxin and modulates formation and cation selectivity of its membrane channels.