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Quantitating denaturation by formic acid: Imperfect repeats are essential to the stability of the functional amyloid protein FapC

biorxiv. 2020; 
Line Friis Bakmann Christensen,  Jan Stanislaw Nowak,  Thorbjørn Vincent Sønderby,  Signe Andrea Frank, Daniel Erik Otzen
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Molecular Biology Reagents Accordingly, a pET28(+) expression vector was produced by Genscript (Piscataway, NJ) to express the 101-amino acid (aa) S6 from Thermus thermophilus containing the mutations Met1Cys and Phe97Cys (S6M1C, F97C). Get A Quote

摘要

Bacterial functional amyloids are evolutionarily optimized to aggregate to help them fulfil their biological functions, e.g. to provide mechanical stability to biofilm. Amyloid is formed in Pseudomonas sp. by the protein FapC which contains 3 imperfect repeats connected by long linkers. Stepwise removal of these repeats slows down aggregation and increases the propensity of amyloids to fragment during the fibrillation process, but how these mechanistic properties link to fibril stability is unclear. Here we address this question. The extreme robustness of functional amyloid makes them resistant to conventional chemical denaturants, but they dissolve in formic acid (FA) at high concentrations. To quantify th... More

关键词

Functional amyloid, protein stability, fibril, formic acid, protein denaturation, thermodynamics, FapC, Pseudomonas, m-values, heat capacity.