Molecular Dynamics Study of the Cu 2+ Binding-Induced “Structuring” of the N-Terminal Domain of Human Prion Protein
✍ Scribed by Valensin, Gianni; Molteni, Elena; Valensin, Daniela; Taraszkiewicz, Magdalena; Kozlowski, Henryk
- Book ID
- 125893259
- Publisher
- American Chemical Society
- Year
- 2009
- Tongue
- English
- Weight
- 161 KB
- Volume
- 113
- Category
- Article
- ISSN
- 0022-3654
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## Abstract In the physiological form, the prion protein is a glycoprotein tethered to the cell surface via a C‐terminal glycosylphosphatidylinositol anchor, consisting of a largely α‐helical globular C‐terminal domain and an unstructured N‐terminal portion. This unstructured part of the protein co
We have carried out molecular dynamics simulation of the N-terminal domain of the repressor protein in a surrounding environment including explicit waters and ions. We observe two apparent dynamics substates in the nanosecond protein simulation, the transition occurring around 500 ps. The existence