By virtue of its quantitative nature, NMR spectroscopy is increasingly becoming the method of choice to monitor a reaction and determine its kinetic parameters. We’ve demonstrated the ability of the NMReady-60 to monitor a reaction and subsequently extract kinetic parameters in a previous blog post. In this blog post, I’d like to show how the NMReady-60 can be used to study enzyme kinetics. Adapted from a Journal of Chemical Education article published by Olsen and Giles, the enzymatic hydrolysis of N-acetyl-DL-methionine by porcine acylase was studied.

Nucleophilic substitution reactions are frequently performed as an experiment in undergraduate organic chemistry courses. Reactions taking place at saturated carbons are mainly classified as SN1 or SN2, where S stands for substitution, N for nucleophilic, and the number indicates the molecularity of the reaction (1 for a unimolecular process, 2 for a bimolecular process). In the SN2 reaction the attack of the nucleophile and elimination of the leaving group occur simultaneously in a concerted process and its rate is proportional to the concentration of both the alkyl halide and the nucleophile.

NMR spectroscopy, as it is typically discussed, or at least how it is initially taught, tends to refer to static systems.  Chemical shifts, integrations and multiplicities are typically reported on

Incorporation of NMR spectroscopy into an undergraduate lab provides an excellent method with which to provide students with practical experiments acquiring their own data and interpreting actual NMR spectra.