Dresden 2003 – wissenschaftliches Programm

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SYCN: Computational nanoscience - from materials to biology

SYCN 102: Computational Nanoscience: From Materials to Biology (Poster, gemeinsam mit SYSE)

SYCN 102.22: Poster

Dienstag, 25. März 2003, 19:00–21:00, ZEU/160

Copper(II) Binding to Prion Protein Octapeptide Studied by Density Functional Methods — •Andreas Weiss and Paul Tavan — Chair for BioMolecular Optics, University of Munich, Germany

It is well known that N-terminal fragments of PrP^C bind Cu(II) ions.Furthermore copper binding seems to be essential for the physiological function of PrP^C and may also be involved in the conformational transition required for generation of infectious PrP^Sc. The overall 3D structure of PrP^C has not yet been fully established, since in aqueous solution at low pH and in the absence of bound Cu(II) ions the N-terminus is a random coil. In the presence of Cu(II), however, the N-terminal octapeptide repeat region could assume a well-defined 3D structure. We have carried out a series of DFT calculations on models of Cu(II) bound to the corresponding octapeptides as to structurally interpret EXAFS, EPR and ENDOR experiments conducted by our partners [1,2] in a cooperative research effort [3].

[1] F. Parak et al., TU München.
L. Moroder et al., Max-Planck-Institut für Biochemie, Martinsried.
Bayerischer Forschungsverbund Prionen: Cu(II)-Bindung des PrPC: Einfluss auf Struktur, Konformationsdynamik und Infektiosität. P. Tavan, LMU München, H. Kretzschmar, LMU München, L. Moroder, Max-Planck-Institut für Biochemie, Martinsried, F. Parak, TU München.