N-terminal protein tails act as aggregation protective entropic bristles: The SUMO case

Ricardo Graña-Montes, Patrizia Marinelli, David Reverter, Salvador Ventura

Research output: Contribution to journalArticleResearchpeer-review

25 Citations (Scopus)


The formation of β-sheet enriched amyloid fibrils constitutes the hallmark of many diseases but is also an intrinsic property of polypeptide chains in general, because the formation of compact globular proteins comes at the expense of an inherent sequential aggregation propensity. In this context, identification of strategies that enable proteins to remain functional and soluble in the cell has become a central issue in chemical biology. We show here, using human SUMO proteins as a model system, that the recurrent presence of disordered tails flanking globular domains might constitute yet another of these protective strategies. These short, disordered, and highly soluble protein segments would act as intramolecular entropic bristles, reducing the overall protein intrinsic aggregation propensity and favoring thus the attainment and maintenance of functional conformations. © 2014 American Chemical Society.
Original languageEnglish
Pages (from-to)1194-1203
Publication statusPublished - 14 Apr 2014


Dive into the research topics of 'N-terminal protein tails act as aggregation protective entropic bristles: The SUMO case'. Together they form a unique fingerprint.

Cite this