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

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

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

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

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

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

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

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.

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.

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

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

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

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

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

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

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.

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 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.

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

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

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

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

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

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

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

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

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

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

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

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

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

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