Primary Structure: Peptide bonds form between the carboxyl and amino groups of adjacent amino acids, forming a long polypeptide chain.
Secondary Structure: Reactions and interactions, such as hydrogen bonding, take place between carboxyl and amino groups along the backbone of the polypeptide. This is how structures like alpha helixes and beta sheets are formed
Tertiary Structure: Reactions and interactions take place between residue groups (aka. R groups/side chains) of amino acids, giving the protein its specific structure for its purpose. Examples of these reactions include hydrogen bonds, ionic bonds, and disulphide bridges.
Quaternary Structure: This occurs in proteins with multiple subunits (such as haemoglobin, which has four). The subunits come together to form the final protein which is ready to be processed and packaged for secretion from the cell.