Thermodynamics of α‐Chymotrypsin‐Inhibitor Complex Formation

Abstract

The temperature dependence of the association constant (Ki) of the α-chymotrypsin active centre interaction with some aromatic and aliphatic compounds has been studied (at pH 8.0). The following results are discussed: 1 It was found that log Ki is linearly dependent on 1/T over the 0–30° range. 2 The enthalpy of binding of the benzene derivatives studied was observed to be approximately equal to –4.5 kcal/mole. 3 The enthalpy increment of the enzyme-inhibitor complex formation for any aliphatic hydrocarbon fragment of inhibitor molecule is near to zero.