Abstract:
:The hydrogen exchange kinetics of the complex of trypsin-soybean trypsin inhibitor (Kunitz) have been compared to the calculated sum of the exchange kinetics for the inhibitor and trypsin measured separately. The exchange rates observed for the complex are substantially less than the sum of the exchange rates in the two individual proteins. These results cannot be accounted for by changes in intermolecular or intramolecular hydrogen bonding. The decrease in exchange rates in the complex are ascribed to changes in solvent accessibility in the component proteins.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Woodward CK,Ellis LMdoi
10.1021/bi00686a020subject
Has Abstractpub_date
1975-07-29 00:00:00pages
3419-23issue
15eissn
0006-2960issn
1520-4995journal_volume
14pub_type
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