Final answer:
The net charge of the peptide at pH 2 is positive, at pH 7 it is close to zero, and at pH 10 it is negative.
Step-by-step explanation:
The net charge of the peptide at different pH values can be determined by considering the ionization states of the amino acids in the peptide and their pKa values. At pH = 2, all the carboxylic acid groups (COOH) in the peptide will be protonated (pKa ~ 2) and have a positive charge. The amino groups (NH3+) of lysine (K) and arginine (R) will also be protonated and have a positive charge. Therefore, the net charge at pH = 2 will be positive.
At pH = 7, the carboxylic acid groups will be deprotonated and have a negative charge, while the amino groups will be protonated and have a positive charge. However, the net charge will be close to zero because the pKa values of the amino acids in the peptide are around 2 and 9, resulting in roughly equal amounts of protonated and deprotonated forms.
At pH = 10, the carboxylic acid groups will be deprotonated and have a negative charge, while the amino groups will also be deprotonated and neutral. Thus, the net charge will be negative.