Chemistry of Amino Acids in Medical Studies Quiz

Amino acids are building blocks (or monomers) of proteins.

Studying amino acids helps us understand the structure/function relationship of many biomolecules, such as hormones and the primary structure of insulin.

Stereochemistry in amino acids refers to the D & L isomers, which determine the spatial arrangement of the groups, making amino acids tetrahedral in nature.

Amino acids are classified based on their side chain properties, such as nonpolar, polar, acidic, and basic.

Amino acids can act as both acids and bases, due to the presence of both an amino group and a carboxylic acid group.

Amino acids undergo titration behavior due to the presence of both acidic and basic functional groups.

Stereochemistry refers to the ‘‘handedness’’ of a molecule and it is used to name the enantiomer of a chiral compound.

The D,L-nomenclature based on D- and L-glyceraldehyde relative to the position of the α-amino group is preferred.

The seven types of amino acids classified based on structure are aliphatic, hydroxy, sulfur-containing, dicarboxylic acid and their amides, diamino, aromatic, and imino or heterocyclic amino acids.

An example of an aliphatic amino acid is Alanine.

The category of hydroxy amino acids includes Serine, Threonine, and Tyrosine.

Proline differs from other amino acids in that it contains an imino group, rather than an amino group.

The two major classes are hydrophilic or polar amino acids, and hydrophobic or nonpolar amino acids.

The D,L-nomenclature system is based on D- and L-glyceraldehyde relative to the position of the α-amino group.

Fischer’s projection is a simple representation used in stereochemistry, where the longest chain is oriented vertically and the more highly oxidized carbon is at the top.

D-forms of amino acids are only present in some antibiotics and in bacterial cell walls.