1. Distribute the 15 tacks randomly, but evenly along the toober. The tacked toober represents a protein made of 15 amino acids.
   
2. Fold you protein, following the laws of chemistry that drive protein folding:

Teaching Tips:

Students should have no trouble folding their toober so that all of the yellow, hydrophobiuc tacks are clustered together in the central core of the folded structure. However, it may be difficult to maintain this structure while simultaneously:

• Pairing up blue and red tacks (positive and negative charges that neutralize each other).
• And pairing orange tacks that form disulfide bonds
• And keeping all the polar white tacks on the surface of the protein.

So, after everyone had folded their toober as best they can, the teach can point out:

• Every toober had a different random sequence of tacks (amino acids) and therefore each toober (protein) folded into a different structure.
• Some sequences of tacks were more easily folded into a reasonable structure than others. In fact, the 30,000 proteins encoded by the human genome have been selected from an enormous number of possible amino acid sequences based on their ability to spontaneously fold into a stable structure that simultaneously satisfies these basic laws of chemistry.

For more suggestions about how to teach concepts of molecular structure and function, visit the MSOE Center for BioMolecular Modeling website, http://www.rpc.msoe.edu/cbm and check out the CBM summer course entitles Genes, Schemes and Molecular Machines.