
%0 Journal Article
%A Tsavalos, M 
%A Nicholson, BC 
%A Spotswood, TM 
%T <sup>19</sup>F nuclear magnetic resonance studies of the interaction of inhibitors with chymotrypsin. Ring-fluorinated derivatives of N-trifluoroacetylphenylalanine
%J Australian Journal of Chemistry
%D 1978/10/01
%V 31
%N 10
%P 2179-2186
%K 
%R https://doi.org/10.1071/CH9782179
%U https://www.publish.csiro.au/paper/CH9782179 
%X The complexes formed between chymotrypsin and the doubly fluorine- labelled inhibitors, o-, m- and p-fluoro-N-trifluoroacetyl-D- phenylalanine and 2,4-difluoro-N-trifluoroacetyl-D-phenylalanine, have been characterized by 19F N.M.R. spectroscopy and binding parameters, &#916;B and KI, have been derived. The results confirm the importance of the amido binding site in orienting aromatic amino acids at the active site of chymotrypsin. Changes in &#916;B, the change in chemical shift of the enzyme-bound inhibitor, are shown to be a very sensitive probe of enzyme-inhibitor interactions. 
