2009 Fiscal Year Final Research Report
Supramolecular structural analysis of the pore forming protein
| Project/Area Number |
20780077
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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 |
Applied biochemistry
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| Research Institution | Nagasaki University |
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Principal Investigator |
GODA Shuichiro Nagasaki University, 工学部, 准教授 (00346587)
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| Project Period (FY) |
2008 – 2009
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| Keywords | タンパク質 / 構造変化 / レクチン / 溶血性 / X線小角散乱 |
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| Research Abstract |
To elucidate the pore forming oligomeric structure of the hemolytic lectin derived from sea invertebrate Cucumaria echinata, small-angle x-ray scattering and circular dicolorism(CD) were carried out. CEL-III forms 25-mer in artificial oligomerization solution, but it dissociate into hexamer in the presence of detergent. This suggests that the hexamer is minimum unit of hemolytic activity. Kratky plot showed that the tertiary structure of CEL-III was destroyed and spectra were similar to that of the random coil structure in the absence of Ca^(2+)or lacturose or both. Whereas, CD spectra showed that the secondary structure was almost same as monomeric CEL-III under the same condition. These results suggest that the tertiary structure of CEL-III under the oligomerization was almost destroyed, but still contains same secondary structure as monomeric CEL-III.
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