Bétaszsheet

Bétaszsheet is a term sometimes used colloquially to refer to a beta-pleated sheet secondary structure found in proteins. Beta-pleated sheets are a common structural motif in proteins, alongside alpha-helices. They are formed by hydrogen bonds between backbone atoms of adjacent polypeptide chains or different segments of the same chain. These hydrogen bonds occur between the carbonyl oxygen of one amino acid residue and the amide hydrogen of another.

There are two main types of beta-pleated sheets: parallel and antiparallel. In an antiparallel beta-pleated sheet, the adjacent polypeptide strands run in opposite directions, meaning their N-termini and C-termini are aligned. In a parallel beta-pleated sheet, the adjacent strands run in the same direction. The hydrogen bonds in antiparallel sheets are more linear and thus stronger than those in parallel sheets, which are angled.

Beta-pleated sheets contribute to the overall three-dimensional structure and stability of proteins. They can form rigid, planar structures and are often found in the core of globular proteins or as the main structural element in fibrous proteins like silk. The specific arrangement and number of beta-strands within a beta-pleated sheet can vary widely, leading to diverse protein functions. The term "bétaszsheet" is a less formal variation of the standard scientific nomenclature.