English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

We have performed molecular dynamics simulations on the human prion protein to study the effect of point mutations in relation to the inherited form of Creutzfeldt-Jakob disease. Three model structures of the human prion protein are examined with a focus on their dynamics and conformational changes. Model 1 is an NMR structure of the globular domain (125-228) of a wild-type prion. The model consists of three -helices and an anti-parallel -sheet. Models 2 and 3 are mutant structures containing a Glu200Asp and a Glu200Lys substitution, respectively. These models are derived from NMR structures. The Glu200Lys mutation in model 3 is a disease-related amino acid exchange. The results of about 2-million time step calculations have shown that the globular domains of models 1 and 2 are stable, whereas, for model 3, we observe a partial unfolding and reorganization of the protein structure by insertion of the disease-related mutation Glu200Lys.

MD Simulations on the Influence of Disease-Related Amino Acid Mutations in the Human Prion Protein