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- W2789914061 abstract "Free energy landscapes of proteins have been theoretically predicted to be extremely complex, wherein protein folding/unfolding occurs in a parallel flow process via multiple intermediates separated by small and large energy barriers. However, not only have such complexities been rarely observed in ensemble measurements of folding/unfolding of proteins, how such underlying complexities in free energy landscapes modulate their aggregation propensities lack detailed understanding. Here, a comparative study of the folding pathways of the mouse prion protein was carried out at two solvent conditions: low pH where the protein is destabilized and aggregation-prone; and in physiological conditions where the protein does not normally aggregate, unless destabilized. In physiological conditions, the protein utilizes a single pathway to fold via two obligatory intermediate states. However, kinetic folding studies in aggregation-prone solvent conditions reveal an unusually complex energy landscape. Folded and unfolded protein molecules are observed to traverse different, distinct regions of the energy landscape of the protein. The thermodynamic states accessible on the folding pathway are not accessible to the unfolding pathway and vice versa as they are separated by large energy barriers that render the two folding pathways inaccessible to each other. Consequently, the folding/unfolding pathway utilized depends on the initial folding conditions i.e. on where on the energy landscape the folding/unfolding commences from. This energetic frustration channelizes the native protein to unfold to the denatured state via an intermediate previously identified to be the monomeric precursor conformation initiating misfolding of the prion protein. This study proposes a plausible mechanism by which frustration and ruggedness in a protein's free energy landscape determines the aggregation propensity of the protein." @default.
- W2789914061 created "2018-03-29" @default.
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- W2789914061 date "2018-02-01" @default.
- W2789914061 modified "2023-10-18" @default.
- W2789914061 title "pH-Induced Frustration in the FREE Energy Landscape Dictate Misfolding of the Prion Protein" @default.
- W2789914061 doi "https://doi.org/10.1016/j.bpj.2017.11.2298" @default.
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