National Cheng Kung University, Taiwan
Title: Studying Conformational Changes on GDP and GTP Binding with a Novel Visualization Platform
Biography: Darby Tien-Hao Chang
In many biological processes, proteins have important interactions with various molecules such as proteins, ions or ligands. Many proteins undergo conformational changes upon these interactions, where regions with large conformational changes are critical to the interactions. Several important proteins, such as the universal translation initiation factor (IF2/eIF5B), have been observed having large conformational changes on GDP and GTP binding. This work uses a novel platform, CCProf, to analyze conformational changes of entire proteins. This study analyzes protein conformational change with nine biological features, including 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 well-aligned view so that researchers can capture important relevance between different biological features visually. This analysis help researchers to study potential causes of conformational changes. The results of this work show two flexible regions with disorder-to-order transitions. The large conformational changes of these regions help to recognize multiple binding targets.