| Budget Amount *help |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2018: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2017: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2016: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Outline of Final Research Achievements |
Understanding the relationship between the amino acid sequence of a protein and its native structure is not only interesting as a genetic code deciphering problem, but also important in terms of medical applications. In this study, we focused on the rewiring technique of known structures, which is one of the methods that can predict the 3D structure of proteins with novel folds. The most important thing of the rewiring technique is to distinguish between physically permissible folds and impossible ones, but until now there has been no standard for distinguishing this. In the present study, we find that the frustration of the local structure rule is the criterion for this. The results are useful not only for three-dimensional structure prediction, but also for target structure selection in rational protein design.
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