Using model peptides, we show that the CAN strategy is compatible with all canonical amino acids (although Met is slightly more prone to oxidation). CAN also greatly accelerates ligation in the context of sterically hindered thioesters. Furthermore, these demonstrations use methyl thioglycolate (MTG) as a slower, relative to MPAA, but desulfurization-compatible thiol additive for NCL. Finally, we illustrate the utility of CAN for CPS by performing a strain-promoted click reaction, NCL, desulfurization, and linker cleavage to produce the E. coli 50S ribosomal subunit L32 in one pot.