Amino Acids in Proteins

Amino acids are categorized based on the polarity of their side chains (R groups). Polar R groups can form hydrogen bonds with water, while non-polar R groups cannot.

Essential amino acids cannot be synthesized by the body and must be obtained from food. Their deficiency impacts health and protein synthesis.

Non-essential amino acids can be produced by the body and are not required in the diet.

Semi-essential amino acids are produced by the body, but insufficiently for optimal health, especially in children.

Amino acids with a benzene ring side chain, like phenylalanine and tyrosine.

Amino acids with a ring structure in their side chains containing atoms other than carbon, such as tryptophan and histidine.

Amino acids with side chains that are polar (hydrophilic) and can form hydrogen bonds with water.

Amino acids with side chains that are nonpolar (hydrophobic) and cannot form hydrogen bonds with water.

Amino acids that enter the metabolic pathway of ketone bodies, meaning they can produce ketone bodies.

The building blocks of proteins, found in all living cells. There are 20 commonly found in proteins.

Large molecules made from long chains of amino acids (polypeptides).

An amino acid where the amino group is attached to the carbon atom next to the carboxyl group.

A type of amino acid with a specific spatial arrangement (left-handed form).

Amino acid molecules have a non-superimposable mirror image, and the alpha carbon (except glycine) has 4 different groups attached to it

Categorization of amino acids based on the structure of their side chain (R group).

Amino acids with non-aromatic, hydrocarbon side chains (not Rings).

Amino acids with benzene ring in their side chains.

A type of amino acid with a non polar side chain, no functional group.

Amino acids with a carboxyl group in their side chain.

Amino acids with an amino group in their side chain.

Amino acids are classified based on their metabolic breakdown products.

These amino acids can be broken down into glucose.

These amino acids can be broken down into ketone bodies.

These amino acids can be broken down into both glucose and ketone bodies.

Amino acids contain a central carbon atom bonded to an amino group, a carboxyl group, a hydrogen atom, and a variable side chain (R group).

Amino acids exist as L- and D- isomers, but only L-isomers are found in proteins.

Amino acids are colorless, crystalline solids, insoluble in nonpolar solvents, and soluble in polar solvents and they have a high melting point.

The ionic form of an amino acid with both a positive and a negative charge at a particular pH (isoelectric point).

The pH at which an amino acid has a net zero charge.

Amino acids can act as both acids and bases.

A chemical test used to detect the presence of amino acids.

A chemical reaction that removes a carboxyl group from an amino acid, producing an amine.

The process where amino acids lose carbon dioxide (CO2) to produce amines.

Histidine transforms into Histamine and releases CO2.

Tyrosine converts to Tyramine while releasing CO2.

Lysine forms Cadaverine and CO2.,

The process where the carboxyl group of an amino acid loses a hydrogen ion (H+).

Reaction between amino acids and alcohols to form esters.

Amino acids link together via condensation to form peptides. Water is released.

A covalent bond formed between cysteine or other sulfur-containing molecules via SH side chains.

Many amino acids join to form polypeptide chains and proteins, through peptide bonds.

Essential for various cellular functions (nerve impulses, synthesis of important molecules).