|M.Sc Student||Danielli Lena|
|Subject||Quantifying Distribution of Protein Oligomerization|
Degree Reflects Cellular Information Capacity
|Department||Department of Biomedical Engineering||Supervisor||Dr. Ramez Daniel|
|Full Thesis text|
Protein’s oligomerization phenomena are well-studied in the scale of a single protein. In this research we extended our study to a genome scale. The results indicate existence of an upper bound for even and odd oligomers frequency in proteome. This upper bound have a characteristics of information capacity and it is repeated in various living organisms.
Generation of information, energy and biomass in living cells involves integrated processes, which optimally evolved into complex and robust cellular networks. Protein homo-oligomerization, which is correlated with cooperativity in biology, is one means of scaling the complexity of protein networks. It can play critical roles in determining the sensitivity of genetic regulatory circuits and metabolic pathways. Therefore, understanding such roles may enable new approaches to probe biological functions. Here, we analyzed the frequency of protein oligomerization degree in the cell proteome for five different organisms, and then, we asked the question if there is a design trade-off between protein oligomerization, information precision and energy cost of protein synthesis. Our results indicate that there is an upper limit for protein oligomerization degree, possibly due to the trade-off between cellular resource limitations and information precision involved in biochemical reaction networks. These findings can explain the principles of cellular architecture design and provide a quantitative tool to scale synthetic biological systems.