Difference between revisions of "Team:BostonU/Modeling"
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<p>The BU iGEM team has relied heavily on modeling as our method for determining where the ideal sites are on proteins for splitting. We focused on two major criteria when choosing split sites. We wanted to make sure that the protein would not be split inn the middle of any secondary structures (alpha helices or beta sheets), and also we tried to choose the most hydrophillic split sites possible. The reasoning for this is that we wanted to make sure that we didn't split at any of the proteins hydrophobic core sites. In order to make sure that we met our criteria for the split sites, we developed a model that takes the amino acid sequence of a protein as input and returns the hydrophobicity of each amino acid and the locations of secondary structures. By graphing the results, we were able to identify regions that we hypothesize are ideal for our protein splitting toolkit.</p> | <p>The BU iGEM team has relied heavily on modeling as our method for determining where the ideal sites are on proteins for splitting. We focused on two major criteria when choosing split sites. We wanted to make sure that the protein would not be split inn the middle of any secondary structures (alpha helices or beta sheets), and also we tried to choose the most hydrophillic split sites possible. The reasoning for this is that we wanted to make sure that we didn't split at any of the proteins hydrophobic core sites. In order to make sure that we met our criteria for the split sites, we developed a model that takes the amino acid sequence of a protein as input and returns the hydrophobicity of each amino acid and the locations of secondary structures. By graphing the results, we were able to identify regions that we hypothesize are ideal for our protein splitting toolkit.</p> | ||
Revision as of 07:13, 3 August 2015
Modeling
The BU iGEM team has relied heavily on modeling as our method for determining where the ideal sites are on proteins for splitting. We focused on two major criteria when choosing split sites. We wanted to make sure that the protein would not be split inn the middle of any secondary structures (alpha helices or beta sheets), and also we tried to choose the most hydrophillic split sites possible. The reasoning for this is that we wanted to make sure that we didn't split at any of the proteins hydrophobic core sites. In order to make sure that we met our criteria for the split sites, we developed a model that takes the amino acid sequence of a protein as input and returns the hydrophobicity of each amino acid and the locations of secondary structures. By graphing the results, we were able to identify regions that we hypothesize are ideal for our protein splitting toolkit.
