Nuclear Magnetic Resonance Studies of Enzyme-Substrate Interaction

Author: Ault, Bruce Stafford

Year: 1970

Degree: Bachelor's thesis

Advisor: Richards, John H.

Committee Member: Unknown, Unknown

Option: Chemistry

DOI: 10.7907/v1wd-yv82

Abstract

The complex formed by the interaction of N-trifluoro-acetyl- D,L-tryptophan with the enzyme alpha-chymotrypsin was studied. using nuclear magnetic resonance spectroscopy. The effect of the complex formation on the fluorine spectra of the D-isomer of the inhibitor is quite distinct, while no change is apparent with the D-isomer. The D-isomer appeared to be bound much more tightly than was the L-isomer. These results were obtained through studies of the change in line width of the resonance peak, and also studies of the downfield shift of the D-isomer resonance signal. It was shown that the D-isomer was sufficiently strongly bound to shorten the relaxation time by, a factor of ten, and to increase the relative chemical shift of the D-isomer signal by 87 Hertz. The maximum effect occurs at pH 6.4.

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