Journal
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
Volume 7, Issue 7, Pages 1349-1351Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/b502255j
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In the presence of ethanol, insulin forms amyloid morphologically distinct from the ambient specimen. Due to stability of fibrils and the autocatalytic character of the process, the two amyloid templates, when seeded, replicate the initial morphologies ( and inter-beta-strand hydrogen bonding patterns) regardless of the environmental biases, such as the cosolvent presence. Such templated memory'' effect is advantageous in synthesizing structurally uniform protein nanofibrils under conditions favoring alternative wild'' forms. This also appears to parallel prion strains'' phenomenon, suggesting that strains'' may reflect a generic trait in all amyloids including those not associated with disease.
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