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Molecular chaperones play central roles in sustaining protein homeostasis and preventing protein aggregation. Most studies of these systems have been performed in bulk, providing averaged measurements, though recent single-molecule approaches have provided an in-depth understanding of the molecular mechanisms of their activities and structural rearrangements during substrate recognition. Chaperone activities have been observed to be substrate specific, with some associated with ATP-dependent structural dynamics and others via interactions with co-chaperones. This Review aims to describe the novel mechanisms of molecular chaperones as revealed by single-molecule approaches, and to provide insights into their functioning and its implications for protein homeostasis and human diseases. Copyright © 2023 Elsevier Ltd. All rights reserved.

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Ayush Chandrakant Mistry, Debojyoti Chowdhury, Soham Chakraborty, Shubhasis Haldar. Elucidating the novel mechanisms of molecular chaperones by single-molecule technologies. Trends in biochemical sciences. 2024 Jan;49(1):38-51

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PMID: 37980187

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