AMYCO: evaluation of mutational impact on prion-like proteins aggregation propensity.

ABSTRACT:

Background

Around 1% of human proteins are predicted to contain a disordered and low complexity prion-like domain (PrLD). Mutations in PrLDs have been shown promote a transition towards an aggregation-prone state in several diseases.

Results

Recently, we have shown that an algorithm that considers the effects of mutations on PrLDs composition, as well as on localized amyloid propensity can predict the impact of these amino acid changes on protein intracellular aggregation. In this application note, we implement this concept into the AMYCO web server, a refined algorithm that forecasts the influence of amino acid changes in prion-like proteins aggregation propensity better than state-of-the-art predictors.

Conclusions

The AMYCO web server allows for a fast and automate

SUBMITTER: Iglesias V 

PROVIDER: S-EPMC6332698 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature