9) Considering the enzymatic reaction catalyzed by HIV protease: Options A) hydrolysis is the net reaction observed. B) a peptide bond is cleaved on the carboxyl side of a proline residue. C) a serine residue serves as the nucleophile during the catalytic event. D) inhibitors have been designed to covalently link to the active site just like natural substrates do. E) None of the above is true. F) All of the above are true

1. NSF is an enzyme that uses the energy of ATP hydrolysis to disassemble complexes between v-SNAREs and t-SNAREs.a) Why do you suppose such an enzyme is needed?b) If NSF were suddenly inactivated and then the cells were examined a short time later, what types of effects would you expect to see?

Deduce the amino acid sequence of a polypeptide from the following:1. Acid hydrolysis gives Ala2, Arg, Lys2, Met, Phe, Ser22. Carboxypeptidase gives Ala3. Trypsin digestion gives 4 peptides        a) Ala, Arg        b) Lys, Phe, Ser        c) Lys        d) Ala, Met, Ser4. CNBr treatment gives        a) Ala, Arg, Lys2, homoserine, Phe, Ser        b) Ala, Ser5. Thermolysin is a protease that cuts on the N-terminal side of hydrophobic amino acids (substrate preference is Leu, Ile, Phe, Trp, Tyr, Val).  Thermolysin treatment of our polypeptide yields 2 peptides        a) Ala, Arg, Ser        b) Ala, Lys2, Met, Phe, Ser

Carnitine acyltransferase I and II are required for: OA) transporting carnitine in the blood. OB) inserting carnitine into cell membranes. OC) translocation of fatty acids from cytosol to mitochondria. OD) transfer of ammonia to carnitine in the urea cycle.