Publications by authors named "Neharika G Chamachi"
Article Synopsis
- This study explores how the human prion protein (PrP) misfolds into its toxic scrapie form, identifying intermediates like PrP* through extensive molecular dynamics simulations.
- The findings reveal that various temperature-dependent free energy landscapes show multiple metastable states, mainly with high β-content and low α-content, which could contribute to the formation of PrP oligomers.
- The research suggests that non-native interactions help stabilize these misfolded states, highlighting the vulnerable C-terminal regions of prion proteins and their structural relationships.
Misfolding and aggregation of prion proteins are associated with several neurodegenerative diseases. Therefore, understanding the mechanism of the misfolding process is of enormous interest in the scientific community. It has been speculated and widely discussed that the native cellular prion protein (PrP) form needs to undergo substantial unfolding to a more stable PrP state, which may further oligomerize into the toxic scrapie (PrP) form.
View Article and Find Full Text PDFThe pathological forms of prions are known to be a result of misfolding, oligomerization, and aggregation of the cellular prion. While the mechanism of misfolding and aggregation in prions has been widely studied using both experimental and computational tools, the structural and energetic characterization of the dimer form have not garnered as much attention. On one hand dimerization can be the first step toward a nucleation-like pathway to aggregation, whereas on the other hand it may also increase the conformational stability preventing self-aggregation.
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