Single-molecule observations of human small heat shock proteins in complex with aggregation-prone client proteins.

ABSTRACT: Small heat shock proteins (sHsps) are molecular chaperones that act to prevent the aberrant aggregation of misfolded proteins. Whilst it is suggested that sHsps prevent aggregation by binding to misfolded client proteins, the dynamic and heterogeneous nature of sHsps has hindered attempts to establish the mechanistic details of how sHsp-client protein complexes form. Single-molecule approaches have emerged as a powerful tool to investigate dynamic and heterogeneous interactions such as those that can occur between sHsps and their client proteins. Here, we use total internal reflection fluorescence microscopy to observe and characterise the complexes formed between model aggregation-prone client proteins (firefly luciferase, rhodanese and chloride intracellular channel 1 protein), and the h

SUBMITTER: Rice L 

PROVIDER: S-EPMC12203938 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature