Hydrogen exchange kinetics changes upon formation of the soybean trypsin inhibitor-trypsin complex.

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

Biochemistry

journal_title

Biochemistry

authors

Woodward CK,Ellis LM

doi

10.1021/bi00686a020

subject

Has Abstract

pub_date

1975-07-29 00:00:00

pages

3419-23

issue

15

eissn

0006-2960

issn

1520-4995

journal_volume

14

pub_type

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