We want to try to achieve the gold criterion "7. Excellence in Another Area", because few teams use protein structure prediction to guide experimental design.
Taking the suggestions that came from our interviews in Human Practices, we used Swiss model to predict the structure of TDPs and finally we chosen SAHS 33020 and CAHS 106094 as for the experimental parts. Here, we will use this page to give a simple explanation about reason why we choose these two proteins instead of others and how the Human Practices helped us optimized our experiments.
During our human practices, Zhizhong Gong pointed out that there would be more than one genes plays its role during the resistant to extremely environment. Hence, we decided to combine different types of TDPs together to confirm whether the combination of TDPs would have a better function as a protectant in freeze-drying. However, to combine which two was a problem. We found all the protein sequence on uniport then used swiss to predict the structure of each protein. Here are the following results.
In order to understand how to choose the protein by using its sequence and predictive structure, we interviewed with Guangyuan Song who was professional in structural biology. He told us that if the sequence and structure between two proteins have a obvious difference, the function of these two proteins would also be different. So if combine two proteins with different functions, the possibility that their combinations could better protect the bacteria in lyophilization may be increased. Hence, according to the structure we had and his explanation, we chose CAHS 106094 and SAHS 33020 as for experiments. Indeed, we chose cahs 106094 first because it showed the best protection to bacteria during freeze-drying. Then, it is obviously that the structures of CHAS 89226, CAHS 94205 and CAHS 107838 are similar to CHAS 106094. However, SAHS 33020 is quite different. As a result, we chose SAHS 33020 as the second one.