Folding principle of proteins with different 3D structures in spite of high sequence identiry
| Project/Area Number |
26330335
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Life / Health / Medical informatics
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| Research Institution | Ritsumeikan University |
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Principal Investigator |
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| Project Period (FY) |
2014-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2016: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000)
Fiscal Year 2015: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2014: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Keywords | アミノ酸配列相同性 / タンパク質立体構造 / フォールディング部位 / 残基間平均距離統計 / 進化的保存疎水残基 / Ｇｏモデル / 配列相同タンパク質 / フォールディング機構 / 配列解析 / 平均距離統計 / Goモデル / 分子動力学 / Ｇｏ モデル |
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| Outline of Final Research Achievements |
The GA-related proteins which binds to human serum albumin and the GB-related domain, which binds to the constant (Fc) region of IgG were treated in this study. In particular, we treated proteins which share 88%, 95%, and even 98% sequence identity but exhibit different 3D structures, i.e., a 3α bundle structure or a 4β + α structure. An analysis based on inter-residue average distance statistics was used to address this problem in addition to an evolutionary analysis. First of all, our general methods were applied to lysozyme, b-trefoil proteins and so on and their effectiveness was confirmed. Then we applied our method to GA・GB-related proteins. As a result, the essential residues to determine the final structures were identified. Our results confirmed by our Go model simulations.
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Report
(4 results)
Research Products
(12 results)
