Team:CU-Boulder/Model
In order to increase our efficiency, while saving time and resources, the team undertook various techniques in molecular modeling in order to discern the best places to perform point mutations. These three separate mechanisms are discussed in detail below. The 14 mutations that we eventually decided on can be seen here in red. Five of these mutations have been carried over from last year, along with nine new mutations added with this year's project.
One of the first approaches that we took in modeling was the knowledge if the approximate difference in length of our AzoPhe residue between its cis and trans conformation. We can see the individual monomers of our hexameric protein in here.
If we found individual residues that were positioned between individual monomers such that the distance between the two were greater than 6 Angstroms (the overall length of our residue in its cis conformation, and less than 13 Angstroms (the overall length of our residue in the trans conformation), then we can reason that our hexamers will be unable to pack once being activated at this point, leaving us to believe that this would be a good position for a point mutation.
As an example, we can see how this works for one of our point mutations, PhenyAlanine69. We see that when we zoom in, that there is a measured distance of 7.1 Angstroms between our residue of interest and the other monomer. 
