JBC, Vol. 251, Issue 3, 763-768, Feb, 1976
Double-headed protease inhibitors from black-eyed peas. V. Analysis of the energetics of protease-inhibitor interactions
L. S. Gennis
The half-site reactivity of trypsin and chymotrypsin binding to two
double-headed black-eyed pea protease inhibitors a trypsin-chymotrypsin
inhibitor (BEPCI) had a trypsin inhibitor (BEPTI), is explained in terms of
the energetics of these inhibitor-protease interactions. Free energy
diagrams are constructed to facilitate interpretation of the energetics.
Coupling-free energies are calculated to reflect the magnitude of the
interdependence of protease-binding (alloassociation) and inhibitor subunit
interactions (isoassociation). The experiment observation of the
predominance of liganded monomer complexes for the lima bean inhibitor and
the Bowman-Birk soybean inhibitor and the predominance of
half-site-liganded complexes for BEPCI and BEPTI is the direct result of
the magnitudes and signs of the coupling free energies which result from
these protease-inhibitor interactions.
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