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Q52363202-711B2AE0-107E-44A1-A250-F80DF5F2E305
Q52363202-711B2AE0-107E-44A1-A250-F80DF5F2E305
BestRank
Statement
http://www.wikidata.org/entity/statement/Q52363202-711B2AE0-107E-44A1-A250-F80DF5F2E305
Role of Ligand-Driven Conformational Changes in Enzyme Catalysis: Modeling the Reactivity of the Catalytic Cage of Triosephosphate Isomerase.
P2860
Q52363202-711B2AE0-107E-44A1-A250-F80DF5F2E305
BestRank
Statement
http://www.wikidata.org/entity/statement/Q52363202-711B2AE0-107E-44A1-A250-F80DF5F2E305
rank
NormalRank
type
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wasDerivedFrom
c6bd0eb4c89699f815bf7f7e4a3675ccbbf903bf
P2860
Enzyme activation through the utilization of intrinsic dianion binding energy.