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The end product obtained is called dipeptide as it is made up of two amino acids. ![]() When two same or different amino acids combine, this results in the elimination of a water molecule and hence the formation of peptide bonds occurs. Peptide bonds are formed between -COOH and -NH 2 groups. 4 different groups are attached to α-carbon.Īmino acids are linked together via peptide bonds or peptide linkage. The difference lies in the side-chain called the R group. These structures are called zwitterions.Īll 20 naturally occurring amino acids have common structural features – an amino group (-NH3+), carboxylate (-COO-) group and a hydrogen-bonded to the same carbon atom. pH ranging between 4-8, amino acids carry both positive and negative charges and do not create electrical fields in the chemical solution. In acidic solution, pH = less than 4, -COO combines with H+ ions and converts into the -COOH i.e., uncharged form whereas in alkaline solution, pH above 9, ammonium ion (-NH 3 +) loses a H + ion and converts into amino groups (-NH 2). The ⍺-amino acids are called so because they carry an amino group (-NH 2) and a carboxyl group (-COOH) at the α-carbon atom. ![]() The α-amino acids may have other functional groups. On hydrolysis of proteins, α-amino acids are obtained. Based on the position of the amino group concerning carboxyl group, amino acids are classified as α, β, ץ, δ and so on. Chains of amino acids are together through peptide bonds.Īltogether, there are a total of 20 amino acids that combine to form proteins of different structures and functions. In other words, proteins are polymers of amino acids. The major functional groups present in the amino groups include amine (-NH 2), carboxyl (-COOH) and side chain (R group). 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