Similar folds with different stabilization mechanisms: the cases of Prion and Doppel proteins.

ABSTRACT:

Background

Protein misfolding is the main cause of a group of fatal neurodegenerative diseases in humans and animals. In particular, in Prion-related diseases the normal cellular form of the Prion Protein PrP (PrPC) is converted into the infectious PrPSc through a conformational process during which it acquires a high beta-sheet content. Doppel is a protein that shares a similar native fold, but lacks the scrapie isoform. Understanding the molecular determinants of these different behaviours is important both for biomedical and biophysical research.

Results

In this paper, the dynamical and energetic properties of the two proteins in solution is comparatively analyzed by means of long time scale explicit solvent, all-atom molecular dynamics in different temperature conditions

SUBMITTER: Colacino S 

PROVIDER: S-EPMC1574322 | biostudies-literature | 2006 Jul

REPOSITORIES: biostudies-literature