Structural Characterization of Amino-terminal Domain of Caleosin

• Main Authors: Chun-Chun Hung, 洪君君
• Other Authors: Ta-Hsien Lin
• Format: Others
• Language: zh-TW
• Published: 2018
• Online Access: http://ndltd.ncl.edu.tw/handle/4p97xg

碩士 === 國立陽明大學 === 生化暨分子生物研究所 === 107 === The energy in plant tissues is stored in the form of carbohydrates, lipids, and proteins, which are accumulated in oil bodies, starch granules and protein bodies, respectively. The oil body constitutes mainly neutral lipids as the core, which is surrounded by a monolayer of phospholipids with proteins embedded. The oil body proteins found includes oleosin, caleosin, and sterololesin. Caleosin (27 kDa protein) comprises three structural domains, an N-terminal hydrophilic domain, a central hydrophobic anchoring domain (including a comparable proline knot motif), and a C-terminal hydrophilic domain. The Ca2+-binding ability and secondary structure of Cal-N in aqueous solution were characterized by NMR. Our data showed that Cal-N adopted mostly random coil, yet, retained its ability of Ca2+-binding in aqueous solution. The structures of Cal-N in micelles formed with LMPG or LMPC are also characterized by CD. Cal-N adopted more helical structures in both micelles formed with LMPG or LMPC.