Author:
Nicholson BC,Spotswood TM
Abstract
The binding of
N-trifluoroacetyl derivatives of phenylalanine to the enzyme chymotrypsin has
been studied by 19F nuclear magnetic resonance spectroscopy.
Separate resonances are observed for the D- and L- enantiomers in the presence
of chymotrypsin and their difference in chemical shift is dependent on the
molar ratio of inhibitor to enzyme. The results are interpreted in terms of the
known structure of the active site and possible modes of reorientation of the
aromatic ring in its binding site. Approximate and accurate methods of
quantifying the data are discussed and values for the dissociation constant (KI)
of the EI complex, and the change in chemical shift on binding, are reported
for the D-isomers.
Cited by
17 articles.
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