Amino Acids Overview and Classification

Organic compounds that contain a carboxylic acid group, hydrogen, an amino group and a side group known as "R-Group".

Amino acids that can be synthesized by vertebrates from other molecules.

Amino acids that cannot be synthesized by vertebrates and must be obtained from the diet.

A classification of amino acids based on the chemical properties of their side chain, known as the "R-group."

The distinctive side chain of an amino acid that gives it unique properties.

The overall 3D shape of a protein, determined by how amino acids interact.

Interactions between multiple polypeptide chains to form a functional protein.

The process of creating a protein from DNA instructions, involving multiple steps.

A section of DNA containing the instructions for making a specific protein.

The process of converting DNA into mRNA.

An asymmetric molecule that cannot be superimposed on its mirror image.

The alpha carbon of an amino acid is attached to four different groups, making it chiral, so it can exist in two mirror-image forms.

The process where a water molecule is removed to form a bond between two amino acids. This creates a peptide bond.

A long chain of amino acids linked together by peptide bonds.

A single amino acid unit within a polypeptide chain.

Proteins are macromolecules made up of long chains of amino acids linked by peptide bonds.

Proteins can perform a wide variety of functions in the body. They act as enzymes, hormones, antibodies, and are also involved in essential structural roles.

Glycine is an amino acid that does not have optical activity because its alpha carbon has two hydrogen atoms attached to it.

The process of unfolding a protein's structure without breaking peptide bonds, disrupting secondary and tertiary structures but leaving the primary structure intact.

Proteins are vital for growth and repair, carrying out diverse roles in the body as enzymes, structural components, hormones, and antibodies.

The original and fundamental building blocks of proteins, linked together in a chain by peptide bonds.

The arrangement of the polypeptide chain into alpha-helix or beta-sheet configurations, forming the protein's shape.

The three-dimensional shape of the folded protein, including interactions between amino acids, forming specific pockets and binding sites.

The association of multiple polypeptide chains (subunits) to form a larger protein structure.

Proteins that are made up of only amino acids, yielding only amino acids upon hydrolysis.

Proteins that are combined with a non-protein component, forming a complex with an additional functional group.

The central carbon atom in an amino acid, attached to an amino group (-NH3+), a carboxyl group (-COO-), a hydrogen atom, and a unique side chain (R group).

Groups of amino acids that share similar properties, often based on their side chains. These groups include uncharged nonpolar, uncharged polar, acidic, and basic amino acids.

Molecules that exist in two mirror-image forms, called stereoisomers, that are not superimposable.

Amino acids with side chains that do not have a charge at physiological pH. They tend to be hydrophobic and prefer to cluster in the interior of proteins.

Amino acids with side chains that have a partial positive or negative charge. They are hydrophilic and tend to be exposed on the surface of proteins.

Amino acids with side chains that have a negative charge at physiological pH. They are acidic and commonly play roles in catalysis and ion binding.

Amino acids with side chains that have a positive charge at physiological pH. They are basic and can form salt bridges with acidic amino acids.

The unique chemical group attached to the α-carbon of an amino acid. It determines the amino acid's properties and plays a crucial role in its biological function.

Derivatives or degraded products of simple and conjugated proteins.

The linear sequence of amino acids in a polypeptide chain.

Local folding patterns within a polypeptide chain, like alpha-helices and beta-sheets, due to hydrogen bonding.

The overall three-dimensional shape of a protein, determined by interactions between amino acid residues.

The arrangement of multiple polypeptide chains in a protein complex.

The pH at which a protein has a net neutral charge, meaning it doesn't move in an electric field.