Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Chia-jung Karen Lu"'
Publikováno v:
Biochemistry. 43:13648-13656
A series of mutants of chymotrypsin inhibitor 2 (CI2), at residues that interact with the inhibited enzyme subtilisin BPN', were studied to determine the relative importance of intermolecular contacts on either side of the scissile bond. Mutants were
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::632852739cfdd218fc8cb470b6418bfd
https://doi.org/10.1021/bi048797k
https://doi.org/10.1021/bi048797k
Atomic resolution structures of trypsin acyl-enzymes and a tetrahedral intermediate analog, along with previously solved structures representing the Michaelis complex, are used to reconstruct events in the catalytic cycle of this classic serine prote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b91d690609e928696ef2973fbbaba29
https://europepmc.org/articles/PMC1458980/
https://europepmc.org/articles/PMC1458980/
Role of the intramolecular hydrogen bond network in the inhibitory power of chymotrypsin inhibitor 2
Publikováno v:
Biochemistry. 44(18)
A series of mutants of chymotrypsin inhibitor 2 (CI2), at residues involved in intramolecular interactions that shape and constrain the binding loop, were studied to determine their relative importance for inhibition of the serine protease subtilisin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3c24b4eaa0a2fc0b76da39e74453a2f
https://pubmed.ncbi.nlm.nih.gov/15865427
https://pubmed.ncbi.nlm.nih.gov/15865427
Publikováno v:
Biochemistry; 5/10/2005, Vol. 44 Issue 18, p6823-6830, 8p
Publikováno v:
Biochemistry; 11/2/2004, Vol. 43 Issue 43, p13648-13656, 9p