Answers are grounded in this paper and cite their sources.
More than 20 human diseases, including Alzheimer's disease, Parkinson's disease, and prion disease, originate from the deposition of misfolded proteins. These proteins, referred as amyloidogenic proteins, adopt a β-sheet-rich structure when transformed from soluble state into insoluble amyloid fibrils. Amyloid formation is influenced by a number of factors that affect the intermolecular interaction, including pH, temperature, ion strength, and chemical bonds. In this review, we focus on the role of disulfide on the stability, structure, oligomerization, and amyloidogenecity of native folded or unfolded amyloidogenic proteins. The effects of introduced disulfide bonds on the amyloidogenicity of proteins lacking native disulfide are also reviewed.
No takes yet. Share an insight, caveat, or question.
Li et al. (2013) studied this question.
Synapse has enriched 10 related papers. Consider them for comparative context: