ArticleBiophysical journal2002
Folding pathways of prion and doppel.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Assessing the Stability of Biological Fibrils by Molecular-Scale Simulations.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Contact-Based Analysis of Aggregation of Intrinsically Disordered Proteins.Methods in molecular biology (Clifton, N.J.) · 2022Review
- Pseudo-Improper-Dihedral Model for Intrinsically Disordered Proteins.Journal of chemical theory and computation · 2020Article
- Dual binding in cohesin-dockerin complexes: the energy landscape and the role of short, terminal segments of the dockerin module.Scientific reports · 2018Article
- Self-assembly of model proteins into virus capsids.Journal of physics. Condensed matter : an Institute of Physics journal · 2017Article
- Mechanical strength of 17,134 model proteins and cysteine slipknots.PLoS computational biology · 2009Article
- Insights from coarse-grained Gō models for protein folding and dynamics.International journal of molecular sciences · 2009Review
- Selection of optimal variants of Gō-like models of proteins through studies of stretching.Biophysical journal · 2008Article
- Similar folds with different stabilization mechanisms: the cases of Prion and Doppel proteins.BMC structural biology · 2006Article
- Universality classes in folding times of proteins.Biophysical journal · 2003Article
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Authors and funding
4 authors.
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Abstract
The relevance of various residue positions for the stability and the folding characteristics of the prion protein in its normal cellular form are investigated by using molecular dynamics simulations of models exploiting the topology of the native state. These models allow for reproducing the experimentally validated two-state behavior of the normal prion isoform. Highly significant correlations are found between the most topologically relevant sites in our analysis and the single point mutations known to be associated with the arousal of the genetic forms of prion disease. Insight into the conformational change is provided by comparing the folding process of cellular prion and doppel that share a similar native state topology: the folding pathways of the former can be grouped in two main classes according to which tertiary structure contacts are formed first enroute to the native state. For the latter a single class of pathways leads to the native state again through a two-state process. Our results are consistent and supportive of the recent experimental findings that doppel lacks the scrapie isoform and that such remarkably different behavior involves residues in the region containing the two beta-strands and the intervening helix.
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