<p alt="content_add" style="font-size: 18px;"> Our innovative project present a target protein disruption method in order to degrade endogenous target proteins acutely in mammalian cells.To explain and predict the possibilities within the wetlab limits，we built ODE models and applied our measured data to parameters simulation method based on Bayesian parameter estimation to obtain parameters which fits our reality better. We use this model to obtain the relation between the expression time of plasmid and protein degradation rate,making it accessible to future teams who want to incorporate our minds into their designs.Through the modeling ,we understand the reaction mechanism more specifically and obtain how different factors influence the degradation process .This model also offers guidelines on choosing detection point and future clinical application. </p>

There are several variants of   derived from different organisms. In our project, we  . The structure of this protein has been determined with and without  The  a  lobe. The two lobes are positively charged towards the protein core to accommodate the negatively charged RNA. Each of these two lobes contains an RNase domain. At the  main is responsible for target cleavage. In contrast to other  two RNase domains of the NUC lobe are located at the outside of the protein, which is likely the reason collateral cleavage upon activation by binding to a matching target. These two domains have been labeled as red spots in Figure 2 and can be found at the interface between the green and pink domain.