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:
up blue and red tacks (positive and negative charges that neutralize
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
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.