Beta leaflet structure

A beta leaflet structure or beta conformation (e.g. in beta-keratins; see also amyloid, see also prions) is a frequently occurring molecular secondary structure of a protein.

The beta-pleated structure consists of the parallel arrangement of two or more peptide chains connected by fibre bridges. The secondary structure of a protein is understood to be the spatial structure of the amino acid chain without considering the side groups. The secondary structure of a protein can be read from its primary structure (amino acid sequence). This three-dimensional structure of a protein is decisive for its selective function (see protein structure; see immunoglobulin superfamily).

The "beta" in "beta-leaflet structure" does not contain any scientific information, but merely expresses that the beta-leaflet structure, in terms of time, was detected after the alpha-helix structure of proteins. The name leaflet is derived from the three-dimensional structure of the beta leaflet, whose corrugated sheet-like form resembles a regularly folded sheet of paper.

1. Liberski PP (2008) Prion diseases: a riddle wrapped in a mystery inside an enigma.Folia Neuropath 46:93-116.