
TY  - JOUR
A1  - Tsavalos, M 
A1  - Nicholson, BC 
A1  - Spotswood, TM 
T1  - <sup>19</sup>F nuclear magnetic resonance studies of the interaction of inhibitors with chymotrypsin. Ring-fluorinated derivatives of N-trifluoroacetylphenylalanine
JF  - Australian Journal of Chemistry
JO  - Aust. J. Chem.
Y1  - 1978
VL  - 31
IS  - 10
SP  - 2179
EP  - 2186
KW  - 
UR  - https://doi.org/10.1071/CH9782179 
N2  - 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. 
ER  -

