2009 Fiscal Year Final Research Report
Structural investigation of the fibrillation intermediate of β_2-microglobulin by H/D exchange-NMR
| Project/Area Number |
20770122
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Biophysics
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| Research Institution | Ritsumeikan University |
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Principal Investigator |
CHATANI Eri Ritsumeikan University, 薬学部, 助教 (00432493)
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| Project Period (FY) |
2008 – 2009
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| Keywords | タンパク質 / フォールディング / ミスフォールディング / アミロイド線維 / 水素-重水素交換 / NMR / 中間体構造 / 蛍光 |
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| Research Abstract |
Protein misfolding occasionally leads to the formation of supramolecular assemblies known as amyloid fibrils, the deposition of which is associated with over 30 degenerative diseases. One of the most unique and essential properties of amyloid fibrils is their template-dependent growth, which underlies the propagation of pathology of amyloidoses. We have investigated a monomer-fibril complex of β_2-microglobulin formed transiently during the fibril growth by using Trp fluorescence and hydrogen/deuterium (H/D) exchange-NMR methods.
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