Question

3. Explain the afollowing trend for carbocation formation: Draw the relevant resonance structures and provide explanation Eenplafond 4. The proteasome is a macromolecular protease complex that degrades ubiquitylated proteins in cells. This is an essential regulatory function to remove proteins from cells in a controlled manner. However, it has been shown that proteasome levels are higher in some cancer cells and that these increased levels lead to a poor clinical outcome in these patients. Despite the proteasome being essential, proteasome inhibitors are used in the clinic to treat mantle cell lymphoma and multiple myeloma. a) The B5 subunit of the proteasome has chymotrypsin-like activity. The main substrates of chymotrypsin are peptide bonds in which the amino acid N-terminal to the bond is a tryptophan, tyrosine, phenylalanine, or leucine. Draw the mechanism for chymotrypsin- mediated hydrolysis for the following general substrate using serine as the covalent catalyst.

Answer 1

3)

7 L-cro ayo LON 20 since c is 20 carbocation, so it would be less slable than A,B because the induch've effect (+9) in case q AB will be mode than e. | A is more stable than & because in case of resonance stalih |-zaków is possible which is abeus in B accounting for ik more slability to r y