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(→Seminar by Prof. Koichi Kato (15.09.2008)) |
(→Seminar by Dr. Hélène Van Melckebeke (16.01.2009)) |
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===== Seminar by Dr. Hélène Van Melckebeke (16.01.2009) ===== | ===== Seminar by Dr. Hélène Van Melckebeke (16.01.2009) ===== | ||
| − | '''High resolution structure of the HET-s(218-289) prion amyloid fibrils using solid-state NMR''' | + | ;'''High resolution structure of the HET-s(218-289) prion amyloid fibrils using solid-state NMR''' |
| − | ''Dr. Hélène Van Melckebeke, Physical Chemistry, ETH Zürich, Switzerland'' | + | ;''Dr. Hélène Van Melckebeke, Physical Chemistry, ETH Zürich, Switzerland'' |
| − | Prions and amyloid fibrils are associated with several animal and human diseases. Despite the paramount importance of the structural aspects, no atomic resolution structure of a prion in its fibrillar state has been reported yet. Solid-state NMR is to date the only technique capable of obtaining the structure of such non-crystalline and non-soluble compounds. | + | ;Prions and amyloid fibrils are associated with several animal and human diseases. Despite the paramount importance of the structural aspects, no atomic resolution structure of a prion in its fibrillar state has been reported yet. Solid-state NMR is to date the only technique capable of obtaining the structure of such non-crystalline and non-soluble compounds. |
We have obtained the structure of amyloid fibrils produced in vitro from the prion-forming domain (residues 218-289) of the HET-s prion from the filamentous fungus Podospora anserina using solid-state NMR techniques. These results give a structural explanation of the stability of the HET-s(218-289) fibrils. In the presentation, both methodological and structural aspects will be discussed. | We have obtained the structure of amyloid fibrils produced in vitro from the prion-forming domain (residues 218-289) of the HET-s prion from the filamentous fungus Podospora anserina using solid-state NMR techniques. These results give a structural explanation of the stability of the HET-s(218-289) fibrils. In the presentation, both methodological and structural aspects will be discussed. | ||
| − | Wasmer, C. Lange, A., Van Melckebeke, H., Siemer, A. B., Riek, R. & Meier, B. H. (2008). Amyloid fibrils of the HET-s(218–289) prion form a β solenoid with a triangular hydrophobic core. Science 319, 1523–1526. | + | ;Wasmer, C. Lange, A., Van Melckebeke, H., Siemer, A. B., Riek, R. & Meier, B. H. (2008). Amyloid fibrils of the HET-s(218–289) prion form a β solenoid with a triangular hydrophobic core. Science 319, 1523–1526. |
== 2008 == | == 2008 == | ||
Revision as of 17:51, 21 January 2009
Contents |
2009
Seminar by Dr. Hélène Van Melckebeke (16.01.2009)
- High resolution structure of the HET-s(218-289) prion amyloid fibrils using solid-state NMR
- Dr. Hélène Van Melckebeke, Physical Chemistry, ETH Zürich, Switzerland
- Prions and amyloid fibrils are associated with several animal and human diseases. Despite the paramount importance of the structural aspects, no atomic resolution structure of a prion in its fibrillar state has been reported yet. Solid-state NMR is to date the only technique capable of obtaining the structure of such non-crystalline and non-soluble compounds.
We have obtained the structure of amyloid fibrils produced in vitro from the prion-forming domain (residues 218-289) of the HET-s prion from the filamentous fungus Podospora anserina using solid-state NMR techniques. These results give a structural explanation of the stability of the HET-s(218-289) fibrils. In the presentation, both methodological and structural aspects will be discussed.
- Wasmer, C. Lange, A., Van Melckebeke, H., Siemer, A. B., Riek, R. & Meier, B. H. (2008). Amyloid fibrils of the HET-s(218–289) prion form a β solenoid with a triangular hydrophobic core. Science 319, 1523–1526.
