Control of conformation of α-chymotrypsin through chemical modification
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00739a025
Reference45 articles.
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2. On the interaction of the active site of α-chymotrypsin with chromophores: Proflavin binding and enzyme conformation during catalysis
3. Chymotrypsinogen A family of proteins. VIII. Thermodynamic analysis of transition I of the methionine sulfoxide derivatives of .alpha.-chymotrypsin
4. Investigations of the Chymotrypsin-catalyzed Hydrolysis of Specific Substrates
5. Physical Evidence for the Existence of at Least Two Salt-dependent Forms of α-Chymotrypsin at Slightly Acid pH
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4. Enzymes as synthetic catalysts: mechanistic and active-site considerations of natural and modified chymotrypsin;Journal of the American Chemical Society;1990-06
5. Recent advances in the use of enzyme-catalysed reactions in organic synthesis;Natural Product Reports;1989
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