Analysis on hydrophobic properties of proteins based on Giraph

DOI

10.2991/amcce-15.2015.247How to use a DOI?

Keywords

analysis on hydrophobic properties; protein; graph model; Giraph

Abstract

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.

Copyright

© 2015, the Authors. Published by Atlantis Press.

Open Access

This is an open access article distributed under the CC BY-NC license (http://creativecommons.org/licenses/by-nc/4.0/).

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TY  - CONF
AU  - Yongyu Fan
AU  - Ruoming He
AU  - Xuesong Wang
PY  - 2015/04
DA  - 2015/04
TI  - Analysis on hydrophobic properties of proteins based on Giraph
BT  - Proceedings of the 2015 International Conference on Automation, Mechanical Control and Computational Engineering
PB  - Atlantis Press
SN  - 1951-6851
UR  - https://doi.org/10.2991/amcce-15.2015.247
DO  - 10.2991/amcce-15.2015.247
ID  - Fan2015/04
ER  -