B. Removing the chorismate substrate from a setup in which the chorismate was bound to chorismate mutase, as shown in part B of the supporting video. In undertaking this unbinding procedure, students were instructed to minimise perturbation to the enzyme's structure by exercising precision and care, so as not to destroy protein secondary structure in the vicinity of the active site. For this purpose, we highlighted in advance three arginine sidechains which we know to be important for the binding of chorismate (shown in the right hand panel of Figure ). This allowed us to highlight to the students those residues which required particular care. C. Starting with chorismate unbound to chorismate mutase, students were asked to dock chorismate into the chorismate mutase active site so that it remained in a bound pose. An example is shown in part C of the supporting video. Again, part of the challenge here is to utilize sufficient care and precision so as to not disrupt the secondary structure of the protein by not introducing too much energy into the chorismate molecule along its docking trajectory.