A proper equilibrium between the production and degradation of proteins is provided by the dimeric co-chaperone carboxyl terminus of Hsp70 interacting protein (CHIP), which is necessary for regular cellular growth and function.
Heat increases chaperone activity in CHIP but not in its isolated domains. We look into the effects of heat and urea on the stability of its domains in this work. While the mutant including the U-box ubiquitin ligase domain was dimeric but had extremely low stability, the deletion mutant having the TPR domain, which binds to the chaperones Hsp70 or Hsp90, was monomeric and displayed similar folding and stability to WT. Compared to the WT protein, the deletion mutants seemed to maintain the majority of their structural integrity, although the areas around the tryptophan residues,
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