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Recent years have witnessed major advances in our understanding of the structural basis of protein aggregation on several fronts.
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Importantly, the general success of these algorithms [85,176] in predicting aggregation-prone regions in intact proteins indicates that short stretches of the sequence might drive the aggregation of the entire polypeptide chain and allows rationalisation of protein aggregation behaviour on the basis of side-chain composition within these specific regions.
(C) Quantitative analysis of protein aggregation in HEK 293T cells.
Vasilescu et al., Porous reduced graphene oxide modified electrodes for the analysis of protein aggregation.
Molecular chaperones and co-chaperones are vital for correct protein folding, inhibition of protein aggregation, and degradation of misfolded proteins.
Chaperones are potent controllers of protein aggregation, promoting protein folding and refolding, and cooperating to degrade irreversibly damaged proteins.
In general, protein glycation can directly affect the formation of protein aggregation.
The structural basis of polyQ-mediated protein aggregation is believed to be the formation of "polar zippers", in which β-sheets are stabilised by hydrogen bonds between polar amino acids [25].
The results underscore the importance of kinetic versus thermodynamic control of S100B protein aggregation.
Hsp16 chaperones act in the cytosol to prevent the aggregation of misfolded and damaged proteins, and appear capable of reversing protein aggregation [ 65- 67].
SG biology represents a compelling example of the biological utility of prion-based protein aggregation.
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