期刊
BIOMACROMOLECULES
卷 15, 期 4, 页码 1194-1203出版社
AMER CHEMICAL SOC
DOI: 10.1021/bm401776z
关键词
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资金
- Ministerio de Ciencia e Innovacion (Spain) [BFU2010-14901]
- AGAUR (Generalitat de Catalunya) [2009-SGR-760]
- ICREA Academia award (ICREA)
- Ministerio de Educacion (Spain) [FPU AP2009-0948]
- AGAUR (Generalitat de Catalunya)
The formation of beta-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.
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