
TY  - JOUR
A1  - Nicholson, BC 
A1  - Spotswood, TM 
T1  - <sup>19</sup>F nuclear magnetic resonance studies of the interaction of inhibitors with chymotrypsin. Derivatives of tryptophan and phenylalanine
JF  - Australian Journal of Chemistry
JO  - Aust. J. Chem.
Y1  - 1978
VL  - 31
IS  - 10
SP  - 2167
EP  - 2177
KW  - 
UR  - https://doi.org/10.1071/CH9782167 
N2  - 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. 
ER  -

