
%0 Journal Article
%A Nicholson, BC 
%A Spotswood, TM 
%T <sup>19</sup>F nuclear magnetic resonance studies of the interaction of inhibitors with chymotrypsin. Derivatives of tryptophan and phenylalanine
%J Australian Journal of Chemistry
%D 1978/10/01
%V 31
%N 10
%P 2167-2177
%K 
%R https://doi.org/10.1071/CH9782167
%U https://www.publish.csiro.au/paper/CH9782167 
%X The binding of the inhibitors N-trifluoroacetyltryptophan, N- trifluoroacetylphenylalanine, N-acetyl-tryptophan and N- acetylphenylalanine to chymotrypsin has been studied by 19F N.M.R. spectroscopy at several pH values. Methods for determining the binding parameters, KI and &#916;B, including a model for enzyme oligomerization and competitive inhibition from a second inhibitor, are discussed and a general non-linear least-squares method is presented. Values of KI and &#916;B are recorded for D and L enantiomers of tryptophan derivatives and for D-phenylalanine derivatives. The results are discussed in terms of a model for the aromatic binding site of chymotrypsin. 
