"

From 2014.igem.org

You do not have permission to edit this page, for the following reason:

You can view and copy the source of this page:

{{:Team:Heidelberg/templates/wikipage_new| title=ENZYME MODELING | white=true | red-logo=true | header-img= | header=background-color:#DE4230 | header-bg=black | subtitle= Modeling of lysozyme activity with product inhibition | container-style=background-color:white; | titles={{:Team:Heidelberg/templates/title|Introduction}} | abstract= The theory of enhancing heatstability by circularization suggests, that the more the ends are constrained, the better stabilization works. Based on this theoretical assumption we identified patterns to have the ability to customly build rigid linkers, that fit between the ends of the protein. Based on over 1000 experimental degradation curves from 9 different constructs with biological and technical replicates of lambda lysozyme, we wanted to gain quantitative insight into the effect of different linkers into the functionality after heatshock. Therefore, a comprehensive approach based on quantitative dynamic modeling (ODEs) was made to determine the relevant information. We started with easy fitting of the data and continued by testing different enzyme kinetics models. We evaluated and identified the most relevant and robust parameters by [[#PLE_analysis|profile likelihood analysis]]. Research suggested that a Michaelis-Menten model with substrate inhibition was appropriate for our data. Our final findings show that circularization of lysozyme can have a considerable influence on enzyme thermostability and that suboptimal linker design can decrease thermostability. These results were extraordinarily important for the calibration of [[Team:Heidelberg/Software/Linker_Software | CRAUT]]. | content= <div class="col-lg-12"> {{:Team:Heidelberg/pages/Enzyme_Modeling_new}} </div> | white-logo= | red= }} {{:Team:Heidelberg/templates/mathjax}}

Return to Team:Heidelberg/Modeling/Enzyme Modeling.