Title
N-Terminal Protein Tails Act as Aggregation Protective Entropic Bristles: The SUMO Case
Author
Ricardo Graña-Montes, Patrizia Marinelli, David Reverter, Salvador Ventura
Year
2014
Journal
Biomacromolecules
Abstract
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.
Full Article
Instrument
FP-8200
Keywords
Fluorescence, Aggregation, Protein structure, Biochemistry