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Q27618131-EFFE1A38-D62D-4B6B-B2B9-4C422A87B704
Q27618131-EFFE1A38-D62D-4B6B-B2B9-4C422A87B704
BestRank
Statement
http://www.wikidata.org/entity/statement/Q27618131-EFFE1A38-D62D-4B6B-B2B9-4C422A87B704
Structural and mutagenesis studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power
P2860
Q27618131-EFFE1A38-D62D-4B6B-B2B9-4C422A87B704
BestRank
Statement
http://www.wikidata.org/entity/statement/Q27618131-EFFE1A38-D62D-4B6B-B2B9-4C422A87B704
rank
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type
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Statement
wasDerivedFrom
cfc746103415e26cd8c85d22657cc934524afd2c
P2860
Stabilization of human triosephosphate isomerase by improvement of the stability of individual alpha-helices in dimeric as well as monomeric forms of the protein.