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A Combined Solid‐State NMR and MD Characterization of the Stability and Dynamics of the HET‐s(218‐289) Prion in its Amyloid Conformation |
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| Authors: | Adam Lange Dr. Zrinka Gattin Hélène Van Melckebeke Dr. Christian Wasmer Alice Soragni Wilfred F. van Gunsteren Prof. Dr. Beat H. Meier Prof. Dr. |
| Affiliation: | Physical Chemistry, ETH Zürich, Wolfgang‐Pauli‐Strasse 10, 8093 Zürich (Switzerland), Fax: (+41)?446‐321‐621 |
| Abstract: | Dynamic and rigid : The prion HET‐s(218–289) consists, in its amyloid form as shown here, of highly ordered and rigid parts and a very dynamic loop, which could be of great importance for fibril formation. Indeed, MD simulations explain the experimental NMR results and describe the dynamics of the salt‐bridge network that stabilizes the amyloid fibril, a feature not easily accessible by experiment.  |
| Keywords: | amyloid fibrils molecular dynamics prions solid‐state structures |