NR ATQR
AU Weiss,A.; Parak,F.G.
TI Structural Instability of the Prion Protein upon Membrane Mimics Revealed by Molecular Dynamics Simulations
QU International Conference - Prion 2005: Between fundamentals and society's needs - 19.10.-21.10.2005, Congress Center Düsseldorf - Poster Session: Structure of PrP and molecular determinants of infectivity STRCT-07
PT Konferenz-Poster
AB
Prions are the causative agents of a class of disease known as transmissible spongiform encephalopathies (TSE). They are composed largely, if not entirely, of pathogenic conformational misfoldings, called PrPsc, of the cellular prion protein PrPc.
The NMR analysis of membrane bound PrPc showed a largely a-helical C-terminus and a flexible N-terminus without well-defined secondary structure.
In spite of many data available from "in vitro" conversion experiments of PrPc to its isoform PrPsc only little is known about the primary events inducing the conformational change.
Molecular dynamics simulations of PrPc using conditions known to induce a conversion to PrPsc in "in vitro" experiments were used to investigate the structural instabilities and possibly the early stages of PrP misfolding.
AD Andreas Weiss, Fritz G. Parak, Physik Department E17, TU München, 85747 Garching, Germany
SP englisch
PO Deutschland