Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)

The unrelated protein Sup35p acts as a release factor during translation termination, and its activity is lost upon amyloid formation. Once Sup35p aggregates, RNA polymerase reads through stop codons, which results in greater protein diversity and the generation of new protein activities that are beneficial for survival. Aggregation of Ure2p and Sup35p are mediated by their disordered, asparagine- and glutamine-rich N-termini. Research into disordered proteins produced significant findings and established important new concepts. On the structural side, novel experimental and computational approaches identified and described disordered protein ensembles and led to terms such as secondary structure propensities, residual structural features, and transient longrange contacts.