| Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2016: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2015: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2014: ¥2,990,000 (Direct Cost: ¥2,300,000、Indirect Cost: ¥690,000)
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| Outline of Final Research Achievements |
Here, we analysed the folding mechanism of immunoglobulin light chain variable domain (VL) which intrinsically have sequence variation, although folded into the same structure. We performed various thermodynamic, kinetic and structural analyses on the monomeric VL that we invented ourselves in another study and clarified the core region for folding of VL. We also found the unexpected heat-induce dimerization for original VL, which instinctively against general idea that dimeric proteins have to dissociate into monomers by heating. We clarified the mechanism of this heat-induce dimerization by a series of thermodynamic analysis. These pieces of information about the folding of VL will be applicable to improve the thermal stability of proteins used in various fields and also provided a significant insight into the development of strategy for prevention, diagnostics and treatment against AL amyloidosis which the amyloid formation by immunoglobulin light chain is associated with.
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