ポスター発表
- 第2日 5月16日（火） P会場（ホワイエ，会議室1004-1007）
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2P-19（3A-S-1415） PDF
プロテオーム試料を基質とした酵素反応における基質タンパク質構造の影響
Enzymatic reactions have been used as tools to analyze proteomic samples. Proteases are employed to digest large proteins into smaller peptides. Protein phosphatases are utilized to remove phosphate groups from proteins, while protein kinases are utilized to add phosphate groups to target proteins. Recently, limited proteolysis has been utilized to map substrate structural changes as it preferentially cleaves surface-exposed domains of proteins. Motivated by this, we conceptualized the use of various enzymes for conformational mapping. We examined the effects of substrate structure on the efficiency of limited reactions with protease, kinase, and phosphatase. As a result, all three enzymes preferred the residues which are more exposed, supporting the possibility of structural profiling of substrate proteins with these enzymatic reactions.