An integrated platform for exploring conformational change of proteins

• Main Authors: Chia-WeiChou, 周家緯
• Other Authors: Tien-Hao Chang
• Format: Others
• Language: zh-TW
• Published: 2014
• Online Access: http://ndltd.ncl.edu.tw/handle/23268556833170679866

碩士 === 國立成功大學 === 電機工程學系 === 102 === Proteins play important roles in many biological processes. These biological processes are conducted by a series of protein interactions with various molecules like proteins, ions or ligands. Many proteins undergo conformational changes upon these interactions, where regions with large conformational changes are critical to the interactions. This work presents the CCProf platform, which provides conformational changes of entire proteins, named conformational change profile (CCP) in the context. CCProf aims to be a platform where users can study potential causes of novel conformational changes. It provides ten biological features, including conformational change, potential binding target site, secondary structure, conservation, disorder propensity, hydropathy propensity, sequence domain, structural domain, phosphorylation site and catalytic site. All these information are integrated into a unified and well aligned view so that researchers can capture important relevance between different biological features visually. CCProf contains 41568 structure pairs for 3638 proteins. In addition, CCProf provides a 3D view in which users can see the structures before and after conformational changes as well as binding targets that induce conformational changes. All information (e.g., CCP, binding targets and structures) shown in CCProf, including intermediate data are available for download to expedite further analyses.