(A) C and D Only
(B) A and D Only
(C) C and E Only
(D) B and E Only
Let's evaluate each statement based on the structural and biochemical properties of amino acids:
Statement A: Correct. Essential amino acids are those that the body cannot synthesize and must be obtained from the diet. Arginine (essential for infants/semi-essential) and Tryptophan are both classified as essential amino acids.
Statement B: Incorrect. Histidine contains an imidazole ring, which is a five-membered heterocyclic ring containing two nitrogen atoms.
Statement C: Incorrect. Proline is a five-membered cyclic ring (pyrrolidine ring) amino acid, not six-membered. It is technically an "imino acid" because its nitrogen is part of the ring.
Statement D: Correct. Glycine (\(NH_2-CH_2-COOH\)) has two hydrogen atoms attached to the \(\alpha\)-carbon. Since it does not have four different groups attached to the \(\alpha\)-carbon, it is achiral (it has no chiral center).
Statement E: Incorrect. The side chain \(MeS-CH_2-CH_2-\) (\(CH_3-S-CH_2-CH_2-\)) belongs to Methionine. Cysteine has a thiol side chain: \(-CH_2-SH\).
Conclusion: Only A and D are true.
Amino acids are divided into two main categories based on dietary requirements:
Except for Glycine, all naturally occurring \(\alpha\)-amino acids are chiral. They exist in two enantiomeric forms (L and D), though only L-amino acids are typically found in proteins.
The "R" group or side chain determines the identity and chemical behavior of each amino acid:
| Amino Acid | Characteristic Side Chain |
|---|---|
| Glycine | \(-H\) (Smallest, Achiral) |
| Cysteine | \(-CH_2SH\) (Forms Disulfide bonds) |
| Methionine | \(-CH_2CH_2SCH_3\) (Thioether) |
| Histidine | Imidazole ring (Heterocyclic) |
| Tryptophan | Indole ring (Heterocyclic/Aromatic) |
| Proline | Secondary amine in 5-membered ring |
Heterocyclic rings contain at least one atom other than carbon (usually Nitrogen or Oxygen) in the ring structure. 1. Histidine: Imidazole. 2. Tryptophan: Indole. 3. Proline: Pyrrolidine.
Because Proline’s side chain is linked back to the nitrogen of the amino group, it has a rigid 5-membered ring structure. This rigidity prevents it from fitting into regular \(\alpha\)-helices of proteins, often causing "kinks" or turns in the protein backbone.
There are only two standard amino acids that contain sulfur: Cysteine and Methionine. Cysteine is highly reactive due to its terminal \(-SH\) group, whereas Methionine is relatively inert because the sulfur is "capped" by a methyl group (thioether).
All chiral amino acids are optically active. This means they can rotate the plane of polarized light. Glycine, being achiral, is the only standard amino acid that is optically inactive.
Expert Contribution by: JEE NEET Experts
Specialists in Biomolecules and Organic Chemistry for competitive exams.