$1)$ How is a eukaryote efficiently using the proteins ERF$1$ and ERF$3$ to recognize stop codons? What steps are involved in this stop codon recognition and peptide release process?

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$2)$ How are misfolded peptides loosely tethered to the chaperonin complex? How does the scientific evidence show that misfolded proteins may escape from the complex? What is the advantage in protein folding for misfolded proteins to escape the chaperonin complex?

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$3)$ How would the deletion of UPF$2$ produce deleterious events in T$-$cell development? How would the observed forms of deleterious events be associated with UPF$2?$ What differentiates cells that are less affected by UPF$2$ deletion from cells that are more affected by UPF$2$ deletion?