Molecular chaperone proteins are involved in a wide range of tasks ranging from facilitating protein folding to general protein stabilisation. A major family of chaperones is the small heat-shock proteins (sHsps).1 sHsps have attracted less research interest than the other chaperones despite their ubiquitous presence in all organisms and their significantly enhanced expression under conditions of cellular stress, for example, elevated temperature. A variety of factors have contributed to this sidelining. Firstly, sHsps are not involved in the highly topical task of protein folding. Rather, they have a primary role in preventing protein aggregation whereby, under stress conditions, they interact with partially folded states of target proteins.
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