Structural Studies on precursor proteins of bioactive peptides to elucidate their maturation.
Project/Area Number |
19570112
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Structural biochemistry
|
Research Institution | Kwansei Gakuin University |
Principal Investigator |
YAMAGUCHI Hiroshi Kwansei Gakuin University, 理工学部, 教授 (10252719)
|
Co-Investigator(Kenkyū-buntansha) |
HIDAKA Yuji 近畿大学, 理工学部, 准教授 (70212165)
|
Project Period (FY) |
2007 – 2009
|
Project Status |
Completed (Fiscal Year 2009)
|
Budget Amount *help |
¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2009: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2008: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2007: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
|
Keywords | X線結晶構造解析 / 結晶構造 / フォールディング解析 / フォールディング中間体 / ウログアニリン / プロウログアニリン / アミロイド前駆体タンパク質 / 蛋白質結晶化 / ペプチドホルモン / 生理活性ペプチド / アミロイド前駆体蛋白質 / 結晶化 / アミロイド前躯体蛋白質 |
Research Abstract |
Prouroguanylin (PUG) is precursor of uroguanylin that is peptide hormone. X-ray crystal structure of PUG has been determined at high resolution. In the folding process of PUG, the structure suggests that not only interactions between proregion and peptide region in the PUG that has correct folding but also those in the folding intermediates are very important. Furthermore, kinetic analysis of a folding process of PUG has been performed. It is elucidated that two folding intermediate structures are important in the folding process. In addition, behaviors of β-amyloid precursor protein in the solution were analyzed by CD, DSC and light scattering.
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Report
(4 results)
Research Products
(44 results)