| Project/Area Number |
26730148
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Life / Health / Medical informatics
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| Research Institution | Tohoku University |
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Principal Investigator |
Shirota Matsuyuki 東北大学, 医学(系)研究科(研究院), 助教 (00549462)
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| Project Period (FY) |
2014-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥3,770,000 (Direct Cost: ¥2,900,000、Indirect Cost: ¥870,000)
Fiscal Year 2015: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2014: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | 蛋白質立体構造 / データベース / 水素結合 / 進化的保存 / 二次構造 / 蛋白質構造 / データベース開発 |
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| Outline of Final Research Achievements |
Although hydrophobic interactions are the driving force of protein folding, polar interactions, such as hydrogen bonds, which buried polar residues make are also important for protein structure and function. However, polar residues that are buried in the protein interior and sequestered from water are considered to be exceptional conformations, whose occurrences, intra-molecular interactions and conservations in natural proteins have not been well studied. In this study, I performed a comprehensive survey of the buried polar residues in the non-redundant protein structures of Protein Data Bank (PDB), focusing on patterns of their side-chain interactions and evolutionary conservation. These results highlight the structural and evolutionary importance of buried polar residues in protein structures and will be beneficial for protein structure prediction and protein design.
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