Final answer:
The newly formed polypeptide is the component that enters the exit tunnel through the large subunit of the ribosome after the tRNA (which was initially in the P site) with the attached growing peptide chain moves to the E site and is expelled without an amino acid.
Step-by-step explanation:
In the given scenario where a tRNA attached to the amino acid lysine enters the ribosome and binds to the growing polypeptide on the other tRNA already present in the ribosome, the component of the complex described that enters the exit tunnel through the large subunit of the ribosome is the newly formed polypeptide. After a peptide bond is formed, the tRNA that held the growing polypeptide chain (tRNA #2) shifts from the A site to the P site in the ribosome, and then as the ribosome continues to advance, this tRNA moves to the E site where it loses its amino acid attachment and is eventually expelled, leaving the ribosome.
The process of translation elongation includes the ribosome moving one codon at a time, allowing a charged tRNA to enter at the A site, the formation of a peptide bond between the amino acid at the A site and the growing polypeptide chain at the P site, followed by the moved tRNA without an amino acid to exit the E site. This cycle repeats as the newly formed polypeptide chain is elongated.