Abstract
The kinetics of the 1H–2H exchange of the peptide groups is studied in 2H2O solutions of the basic pancreatic trypsin inhibitor, of trypsin, and of the inhibitor-trypsin complex. In average the exchange rates in solutions of the complex are slower than the exchange rates in solutions of the constituent proteins. The experimental results are expressed in terms of the probability ϱ of exposure to the solvent of the peptide groups of the proteins, and in the changes in standard free energy ΔG° of the conformational transitions by which the exposure is effected. The distribution of values of these parameters on the peptide groups of the proteins is discussed.
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