secondary sturcture/supersecondary

Super secondary structures

Characteristic combinations of typical secondary structures like alpha helices and beta sheets.

Beta Alpha Beta Unit

Consists of parallel beta sheets connected by an alpha helix, resembling an 'N' shape.

Alpha Alpha Unit

Features two anti-parallel alpha helices, also known as helix-turn-helix, shaped like a 'U'.

Beta Meander

Formed by anti-parallel beta sheets linked by tight reverse turns, creating a meandering pattern.

Greek Key

A structure where a polypeptide chain folds back on itself, resembling a maze.

Motifs

Repetitive super secondary structures, which reveal protein folding but not function.

Domain

A distinct section of a protein that folds and functions independently and can consist of multiple motifs.

Beta Barrel

A series of linked beta meanders, often serving as a transmembrane structure.

Alpha Hemolysin

A pore-forming toxin shaped like a mushroom, released by Staphylococcus aureus, known for its role in staph infections.

Collagen

Composed of three polypeptide chains in a triple helix, known for its strength and organized into water-insoluble fibers.