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

ABSTRACT: Bacterial functional amyloids are evolutionarily optimized to aggregate, so much so that the extreme robustness of functional amyloid makes it very difficult to examine their structure-function relationships in a detailed manner. Previous work has shown that functional amyloids are resistant to conventional chemical denaturants, but they dissolve in formic acid (FA) at high concentrations. However, systematic investigation requires a quantitative analysis of FA's ability to denature proteins. Amyloid formed by Pseudomonas sp. protein FapC provides an excellent model to investigate FA denaturation. It contains three imperfect repeats, and stepwise removal of these repeats slows fibrillation and increases fragmentation during aggregation. However, the link to stability is unclear. We

SUBMITTER: Christensen LFB 

PROVIDER: S-EPMC7489911 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature