Cultivating a Meaningful Application of IMFs through Backward Laboratory Course Design.

This paper describes the development of a first- and second-year inquiry-based laboratory course focused on the development of a meaningful application of intermolecular forces (IMFs). Instead of broad expository coverage of topics, we used backward design: the techniques and concepts for the course were structured around what students are expected to be able to do at the end-individually isolate caffeine from a consumer product as a culminating lab practical, using IMFs to justify solvent choices and determining procedural details. We have found that instructors can select a challenging multilevel experiment that incorporates the application of IMFs in multiple ways and backward design the course so that students are able to complete this experiment individually and autonomously at the end of the semester.

The trimethylammonium headgroup of choline is a major determinant for substrate binding and specificity in choline oxidase.

Choline oxidase catalyzes the oxidation of choline to glycine betaine via two sequential flavin-linked transfers of hydride equivalents to molecular oxygen and formation of a betaine aldehyde intermediate. In the present study, choline and glycine betaine analogs were used as substrates and inhibitors for the enzyme to investigate the structural determinants that are relevant for substrate recognition and specificity. Competitive inhibition patterns with respect to choline were determined for a number of substituted amines at pH 6.