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:'''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''' | ||
Revision as of 17:56, 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.
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 Dr. Hideo Iwai (15.09.2008)
Segmental and fractional isotopic labelling of proteins
Dr. Hideo Iwai, University of Helsinki, Finland
Dr. Iwai will present two new approaches of segmental isotopic labelling and fractional 13C labelling for NMR assignments of proteins. Recently, he has developed a robust approach for segmental isotopic labelling using protein trans-splicing, which could open possibilities to study a domain of intact proteins without dissecting into smaller globular domains. He will also present a novel concept to classify residue types in NMR spectra by the use of fractional labeling, which is distinct from routinely used chemical shifts and spin topologies for identifying residue types.
Dr. Hideo Iwai graduated from the Graduate School of Pharmaceutical Sciences of the University of Tokyo with Prof. Yoji Arata, and received his Ph.D. in 1998 at ETH Zürich, Switzerland, with Prof. Kurt Wüthrich. He then worked as a postdoctoral researcher at ETH Zürich, at the University of Zürich with Prof. Andreas Plückthun, and at RIKEN Genomic Sciences Center in Yokohama, Japan. In 2003 he became Assistant Professor of Chemistry at the University of Saskatchewan in Saskatoon, Canada. Since 2005 he is an Academy Research Fellow at the Institute of Biotechnology of the University of Helsinki in Finland.
