Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
11011827 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2018 | 26 Pages |
Abstract
In this paper, the Sequential Collapse Model (SCM) for protein folding pathways is applied to investigate the location of the non-local contacts in the intrinsically disordered state of α-synuclein, a protein implicated in the onset and spreading of several serious neurodegenerative diseases. The model relies on the entropic cost of forming protein loops due to self-crowding effects, and the protein sequence to determine contact location and stability. It is found that the model predicts the existence of several possible non-local contacts, and the location of the non-local contacts is consistent with existing experimental evidence. The bearing of these findings on the pathogenic mechanism and its regulation is discussed.
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Authors
Fernando Bergasa-Caceres, Herschel A. Rabitz,