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.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Settanni G,Hoang TX,Micheletti C,Maritan Adoi
10.1016/S0006-3495(02)75353-8subject
Has Abstractpub_date
2002-12-01 00:00:00pages
3533-41issue
6eissn
0006-3495issn
1542-0086pii
S0006-3495(02)75353-8journal_volume
83pub_type
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