A bioinformatics method for identifying Q/N-rich prion-like domains in proteins
Numerous proteins contain domains that are enriched in glutamine and asparagine residues, and aggregation of some of these proteins has been linked to both prion formation in yeast and a number of human diseases. Unfortunately, predicting whether a given glutamine/asparagine-rich protein will aggregate has proven difficult. Here we describe a recently developed algorithm designed to predict the aggregation propensity of glutamine/asparagine-rich proteins. We discuss the basis for the algorithm, its limitations, and usage of recently developed online and downloadable versions of the algorithm.
Tandem Repeats in Genes, Proteins, and Disease
Digital Object Identifier (DOI)
Ross, E.D., MacLea, K.S., Anderson, C., and Ben-Hur, A. A bioinformatics method for identifying Q/N-rich prion-like domains in proteins. In Hatters DM and Hannan AJ (eds.), Tandem Repeats in Genes, Proteins, and Disease: Methods and Protocols, Methods Mol Biol, doi:10.1007/978-1-62703-438-8_16, 1017:219-228, 2013.