News

Revision as of 16:54, 21 January 2009

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.

2008

Seminar by Prof. Masatsune Kainosho (14.10.2008)

Recent progress in the SAIL approach to study side-chain conformations of proteins and protein complexes

Prof. Dr. Masatsune Kainosho, Nagoya University and Tokyo Metropolitan University, Japan

Seminar by Prof. Hideo Iwai (15.09.2008)

Seminar by Prof. Koichi Kato (03.07.2008)