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Q27666029-43D21C8B-DAAE-4243-8FB3-22EBF7AE710C
Q27666029-43D21C8B-DAAE-4243-8FB3-22EBF7AE710C
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http://www.wikidata.org/entity/statement/Q27666029-43D21C8B-DAAE-4243-8FB3-22EBF7AE710C
The catalytic aspartate is protonated in the Michaelis complex formed between trypsin and an in vitro evolved substrate-like inhibitor: a refined mechanism of serine protease action
P2860
Q27666029-43D21C8B-DAAE-4243-8FB3-22EBF7AE710C
BestRank
Statement
http://www.wikidata.org/entity/statement/Q27666029-43D21C8B-DAAE-4243-8FB3-22EBF7AE710C
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wasDerivedFrom
217f4cee9f31426df917dfa0005549b0f1a4b18d
P2860
A low-barrier hydrogen bond in the catalytic triad of serine proteases