The secondary structure of each domain is quite different, the N-terminal domain consists of mostly beta pleated sheet, while the C-terminal domain is mostly alpha helical in structure.

Between the outside of the case and an inner lining was a pleated sheet of very thin paper.

Beta sheets consist of beta strands connected laterally by at least two or three backbone hydrogen bonds, forming a generally twisted, pleated sheet.

The alpha sheet (also known as an alpha pleated sheet or a polar pleated sheet) is a hypothetical secondary structure in proteins, first proposed by Linus Pauling and Robert Corey in 1951.

This is due to proton transfer between adjacent molecules in each pleated sheet, rather than molecular rotation.

Specific relief is hilly regions Carpathian, but falling to the eastern extremity of the basin Magurele-Baltesti, is part of a high plain surrounded by hills and rough structures mostly pleated sheet.

Proteins are strings of amino acids that bend naturally in helical loops, hairpin turns and pleated sheets.

Configurations of polypeptide chains with favored orientations of the polypeptide around single bonds: Two pleated sheets.