A bioinformatics method for identifying Q/N-rich prion-like domains in proteins

Methods Mol Biol. 2013:1017:219-28. doi: 10.1007/978-1-62703-438-8_16.

Abstract

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.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Algorithms*
  • Asparagine / genetics
  • Computational Biology / methods*
  • Glutamine / genetics
  • Humans
  • Internet
  • Prions / genetics*
  • Protein Structure, Tertiary
  • Saccharomyces cerevisiae
  • Sequence Analysis, Protein / methods*
  • Software*

Substances

  • Prions
  • Glutamine
  • Asparagine