describe the types of interaction that hold protein molecules in shape: • hydrophobic interactions • hydrogen bonding • ionic bonding • covalent bonding, including disulfide bonds
explain that the maximum rate of reaction (Vmax) is used to derive the Michaelis–Menten constant (Km), which is used to compare the affinity of different enzymes for their substrates
explain the mode of action of enzymes in terms of an active site, enzyme–substrate complex, lowering of activation energy and enzyme specificity, including the lock-and-key hypothesis and the induced-fit hypothesis