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The previous experiments have shown that hydrophobic properties of 20 kinds of human’s amino acid are different. It was of great significance to study whether hydrophobicity of proteins had a role in the research of the intimate relationship of proteins. Besides, it is also very important to balance the proteins’structure and function. Because of the highly complex data produced by hydrophobic proteins, it is suggested to build a computational graph model to solve this problem. In this paper, Giraph platform is used to calculate the data that come from protein interaction database (DIP) . After analyzing the big graph models composed of protein data, this thesis compared the results with those of Cytoscape which is a traditional protein analysis software and finally came to the same conclusions. What’s more, Cytoscape didn’t work when the data of proteins were huge. But Giraph turned out to be more accurate and efficient.

Analysis on hydrophobic properties of proteins based on Giraph