Regulating protein states is considered the core function of chaperones. However, despite their importance to all major cellular processes, the conformational changes that chaperones impart on polypeptide chains are difficult to study directly due to their heterogeneous, dynamic, and multi-step nature. Here, we review recent advances towards this aim using single-molecule manipulation methods, which are rapidly revealing new mechanisms of conformational control and helping to define a different perspective on the chaperone function.


Wruck, F, Avellaneda, M.J, Naqvi, M.M, Koers, E.J, Till, K, Gross, L.D, … Tans, S.J. (2023). Probing Single Chaperone Substrates. In Biophysics of Molecular Chaperones: Function, Mechanisms and Client Protein Interactions, ed. S. Hiller, M. Liu, and L. He (pp. 278–318). RSC. doi:10.1039/BK9781839165986-00278