Robust methods for analyzing trajectories for protein dynamics
| Project/Area Number |
15K00404
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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 | Tottori University |
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Principal Investigator |
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| Co-Investigator(Renkei-kenkyūsha) |
FUJIWARA Shin-ichi 鳥取大学, 医学部, 准教授 (00362880)
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2017: ¥650,000 (Direct Cost: ¥500,000、Indirect Cost: ¥150,000)
Fiscal Year 2016: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
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| Keywords | 構造重ね合わせ / 共分散 / 占有率 / 作業用共分散 / 立体構造 / 重ね合わせ / 分子動力学計算 / 欠損値・欠測値 / 頑健性 |
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| Outline of Final Research Achievements |
Accurate structural superposition is a necessity for studying static and/or dynamic structures of proteins. In this study, we developed a theoretical framework for structural superposition that concerns occupancy factors in crystal structures and off-diagonal components of covariance matrices. The method was implemented as a computer program, mmfitc. It is useful for analyzing, for example, molecular dynamics data, where a great number of structures are subject to. For superposition, we also developed another method which is insensitive to outlier protein molecules to some extent. The method is useful for superposition of a moderate number of structures such as in the case for comparing the crystal structures.
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Report
(4 results)
Research Products
(1 results)
