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The recognition of essential proteins not only can help to understand the mechanism of cell operation, but also help to study the mechanism of biological evolution. At present, many scholars have been discovering essential proteins according to the topological structure of protein network and complexes. While some proteins still can not be recognized. In this paper, we proposed two new methods complex degree centrality (CDC) and complex in-degree and betweenness definition (CIBD) which integrate the local character of protein complexes and topological properties to determine the essentiality of proteins. First, we give the definitions of complex average centrality (CAC) and complex hybrid centrality (CHC) which both describe the properties of protein complexes. Then we propose these new methods CDC and CIBD based on CAC and CHC definitions. In order to access these two methods, different Protein-Protein Interaction (PPI) networks of Saccharomyces cerevisiae, DIP, MIPS and YMBD are used as experimental materials. Experimental results in networks show that the methods of CDC and CIBD can help to improve the precision of predicting essential proteins.
Protein complexes conserved across species indicate processes that are core to cellular machinery (e.g. cell-cycle or DNA damage-repair complexes conserved across human and yeast). While numerous computational methods have been devised to identify co
Essential protein plays a crucial role in the process of cell life. The identification of essential proteins can not only promote the development of drug target technology, but also contribute to the mechanism of biological evolution. There are plent
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