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Induced Dipole–Dipole Interactions Influence the Unfolding Pathways of Wild-Type and Mutant Amyloid β-Peptides
[Image: see text] Amyloid-forming proteins undergo a structural transition from α-helical to disordered conformations and, ultimately, cross-β fibrils. The unfolding and aggregation of the amyloid β-peptide (Aβ) have been implicated in the development and progression of Alzheimer’s disease (AD) and...
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| Vydáno v: | J Phys Chem B |
|---|---|
| Hlavní autoři: | , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
American Chemical
Society
2015
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| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4690986/ https://ncbi.nlm.nih.gov/pubmed/26629591 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/acs.jpcb.5b09978 |
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