Final answer:
Trypsin, a protease that digests proteins, will not directly affect DNA since it is a nucleotide polymer. However, it might digest DNA binding proteins that are associated with DNA, potentially impacting the DNA indirectly.
Step-by-step explanation:
If you treat DNA with trypsin, you might predict that there would not be much of an effect on the DNA itself because trypsin is a protease, an enzyme that digests proteins, and DNA is not a protein. Trypsin cleaves specifically at the carboxyl side of the amino acids lysine and arginine. Since DNA is a polymer of nucleotides, not amino acids, trypsin should not directly degrade DNA. However, if there were any DNA binding proteins associated with the DNA, those could be digested by the trypsin.
For example, if there was a mutation that prevented DNA binding proteins from being produced, the effect would correspond to option (b), where DNA is destroyed by the protease; this would, however, refer to a situation where DNA is left unprotected due to lack of binding proteins and not due to trypsin's direct action on DNA. As for the operator sequence of the trp operon, if it contained a mutation that prevented the repressor protein from binding, it would lead to continuous expression of the operon's genes since the repressor could not inhibit their transcription. Concerning the Avery, Macleod, and McCarty experiments, if proteases prevented the transformation of R strain bacteria, they would have concluded that proteins were the genetic material rather than DNA.