Enzyme-Substrate Interaction by Nuclear Magnetic Resonance

Author: Thompson, Gregory Alan

Year: 1968

Degree: Bachelor's thesis

Advisor: Richards, John H.

Committee Member: Unknown, Unknown

Option: Chemistry

DOI: 10.7907/a2zp-0c39

Abstract

The chemical shifts of the nuclear magnetic resonances of N-acetyl-D-tryptophan are measured and compared to those observed when bound to ∝-chymotrypsin. Chemical shift changes of 1 Hz. are reported for a solution with 1% total substrate bound to the enzyme.

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