"Studying the chaperone function of small heat-shock proteins using sin" by Caitlin Johnston
Small heat-shock proteins (sHsps) are a family of ubiquitous intracellular molecular chaperones that play a vital role in protein homeostasis (proteostasis). It is commonly accepted that these chaperones work by trapping misfolded proteins to prevent their aggregation. However, fundamental questions regarding the molecular mechanisms by which sHsps interact with misfolded proteins remain unanswered. The dynamic and polydisperse nature of mammalian sHsp oligomers has made these chaperones notoriously challenging to study using traditional biochemical approaches. Over the past few decades, singl...