Beta sheet

The β-sheet (also β-pleated sheet) is a common motif of regular secondary structure in proteins. Beta sheets consist of beta strands (also β-strand) connected laterally by at least two or three backbone hydrogen bonds, forming a generally twisted, pleated sheet. A β-strand is a stretch of polypeptide chain typically 3 to 10 amino acids long with backbone in an extended conformation. The supramolecular association of β-sheets has been implicated in formation of the protein aggregates and fibrils observed in many human diseases, notably the amyloidoses such as Alzheimer's disease.

The first β-sheet structure was proposed by William Astbury in the 1930s. He proposed the idea of hydrogen bonding between the peptide bonds of parallel or antiparallel extended β-strands. However, Astbury did not have the necessary data on the bond geometry of the amino acids in order to build accurate models, especially since he did not then know that the peptide bond was planar. A refined version was proposed by Linus Pauling and Robert Corey in 1951. Their model incorporated the planarity of the peptide bond which they previously explained as resulting from keto-enol tautomerization.

The majority of β-strands are arranged adjacent to other strands and form an extensive hydrogen bond network with their neighbors in which the N-H groups in the backbone of one strand establish hydrogen bonds with the C=O groups in the backbone of the adjacent strands. In the fully extended β-strand, successive side chains point straight up, then straight down, then straight up, etc. Adjacent β-strands in a β-sheet are aligned so that their C^α atoms are adjacent and their side chains point in the same direction. The "pleated" appearance of β-strands arises from tetrahedral chemical bonding at the C^α atom; for example, if a side chain points straight up, then the bond to the ${\displaystyle \mathrm {C^{\prime }} }$ must point slightly downwards, since its bond angle is approximately 109.5°. The pleating causes the distance between ${\displaystyle \mathrm {C^{\alpha }} _{i}}$ and ${\displaystyle \mathrm {C_{i+2}^{\alpha }} }$ to be approximately 6 Å, rather than the 7.6 Å (2 × 3.8 Å) expected from two fully extended trans peptides. The "sideways" distance between adjacent C^α atoms in hydrogen-bonded β-strands is roughly 5 Å.

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