CSIR NET Life Science Online Quiz on Biochemistry: Amino Acids | Best Online Test Series for CSIR NET Life Science

Leucine, isoleucine, and valine are all branched-chain amino acids, while proline is not.

Arginine is a precursor to nitric oxide, a signaling molecule involved in vasodilation and immune function.

Phenylalanine has an aromatic side chain, while lysine, serine, and threonine do not.

Glycine is not classified as a polar amino acid, while serine, threonine, and asparagine are.

Serine has a hydroxyl group (-OH) in its side chain, while leucine, cysteine, and asparagine do not.

Glycine is involved in the biosynthesis of heme, a molecule important for oxygen transport in the blood.

Cysteine has a sulfur-containing side chain, while tryptophan, histidine, and glutamate do not.

Histidine is commonly used as a buffer in biological systems due to its ability to act as both an acid and a base.

Proline is not involved in the citric acid cycle, while alanine, aspartate, and glutamate are.

Tryptophan has a cyclic side chain, while asparagine, histidine, and methionine do not.

Glutamic acid is classified as acidic because it has a carboxyl group in its side chain, which can donate a hydrogen ion (proton).

Arginine is not found in collagen, while glycine, proline, and alanine are.

Tryptophan is an essential amino acid and a precursor for serotonin, a neurotransmitter that regulates mood, appetite, and sleep. Tyrosine is a precursor for dopamine and norepinephrine, while methionine is involved in the biosynthesis of other molecules such as S-adenosylmethionine. Phenylalanine is a precursor for tyrosine.

Glycine is not chiral, meaning it does not have a stereocenter and can exist in only one form.

Phenylalanine is not found in hair and nails, while cysteine, methionine, and lysine are.

Lysine is classified as basic because it has an amino group in its side chain, which can accept a hydrogen ion (proton).

Leucine is a major component of muscle tissue and is essential for protein synthesis.

Cysteine has a thiol (-SH) side chain that can form disulfide bonds, which contribute to protein stability.

Proline is commonly found in beta-turns, which are secondary protein structures that reverse the direction of the polypeptide chain.

Proline is a major component of collagen, a fibrous protein that provides structure and support to tissues such as skin, bones, and tendons.

Ornithine is not found in proteins, but it is an important intermediate in the urea cycle.

Essential amino acids cannot be synthesized by the human body and must be obtained from the diet. Lysine, leucine, and phenylalanine are essential amino acids, while proline is not.

Tyrosine is involved in the synthesis of dopamine, a neurotransmitter that plays a role in mood regulation, motivation, and reward.

Glycine is not optically active because it has a hydrogen atom as its side chain, while the other three amino acids have asymmetric carbon atoms in their side chains.

Asparagine and serine have polar side chains that can form hydrogen bonds, while lysine and arginine have basic side chains that do not.

Methionine is not synthesized by plants, while tryptophan, leucine, and tyrosine are.

Proline is not a constituent of hemoglobin, a protein found in red blood cells that carries oxygen throughout the body.

Aspartic acid has a carboxylic acid (-COOH) side chain that can form a salt bridge with a basic side chain.

Glutamic acid is a non-essential amino acid, meaning it can be synthesized by the body.

Arginine is not synthesized from 3-phosphoglycerate, while serine, cysteine, and glycine are.

Tryptophan is involved in the synthesis of serotonin, a neurotransmitter that plays a role in mood, appetite, and sleep.

Cysteine is involved in the formation of disulfide bridges in insulin, which are important for its stability and activity.

Serine, threonine, and tyrosine have hydroxyl (-OH) side chains that can be phosphorylated, while alanine, cysteine and valine do not.