Enzyme-Substrate Interaction by Nuclear Magnetic Resonance
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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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Authors: Gregory Alan Thompson
Institutions: California Institute of Technology