Final answer:
Heat shock proteins act as chaperones that help refold misfolded proteins during thermal stress. They are activated by heat, which promotes dissociation from the NR/HSP complex and induces transcription of their genes, aiding in cellular protection and recovery.
Step-by-step explanation:
During times of thermal stress, heat shock proteins act as chaperones to refold misfolded proteins. Heat serves as a stimulus that facilitates the dissociation of the nuclear receptor from the HSP directly, effectively activating the heat shock proteins. In tandem, transcription of HSP genes is ramped up.
The cellular response to thermal stress involves a focused increase in the transcription of genes coding for heat shock proteins. Their role is crucial in maintaining protein functionality under conditions that promote protein misfolding, such as high temperatures, changes in pH, and exposure to certain chemicals. Essentially, heat shock proteins aid in the protection and recovery of the cell by ensuring that proteins fold properly and maintain their functional shapes under stress conditions.