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A peptide bond forms between the carboxyl group of one amino acid and the amino group of the adjacent amino acid.
I hope this helps. Good luck, (:
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The reaction to form a peptide bond is drawn here:
The -COOH group of one amino acid reacts with the NH2 group of the other, one molecule of water is released (the OH from the COOH group and one of the hydrogen molecules from the NH2 group) and a peptide group is formed (CONH).
The reactants are whatever goes into the reaction (usually they're written on the left of the equation) and the products are usually written on the right. In the above drawing, the reactants are on top, and the product is on the bottom.
If you're given a drawing of a polypeptide, look for the peptide group (a a C double bonded to an O and single bonded to an N). Break the bond between the C and the N. On the C, replace that bond with an -OH and on the N, replace it with a H.
One molecule of water is required per peptide bond. So, in a dipeptide, there's one peptide bond, so one molecule of water is needed to completely hydrolyze the peptide. If the polypeptide had 4 amino acids, you'd need 3 molecules of water and so on.