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Q34351484-6F11E024-2B9E-4B60-BA1E-BE8A03954990
Q34351484-6F11E024-2B9E-4B60-BA1E-BE8A03954990
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http://www.wikidata.org/entity/statement/Q34351484-6F11E024-2B9E-4B60-BA1E-BE8A03954990
Conformational change in the C-terminal domain is responsible for the initiation of creatine kinase thermal aggregation
P2860
Q34351484-6F11E024-2B9E-4B60-BA1E-BE8A03954990
BestRank
Statement
http://www.wikidata.org/entity/statement/Q34351484-6F11E024-2B9E-4B60-BA1E-BE8A03954990
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wasDerivedFrom
f9035977e78c1103920675b4de87d89868346b3d
P2860
Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition.