The protein configuration resulting from the alignment of multiple adjacent beta strands and the formation of hydrogen bonds between them.
Preferentially called a beta pleated sheet; a regular structure in an extended polypeptide chain, stabilised in the form of a sheet by hydrogen bonds between CO and NH groups of adjacent (parallel or antiparallel) chains.
A common secondary structure of a protein, in which several beta strand (or elongated) regions of a protein line up next to each other to form a flat sheet structure.
A three dimensional arrangement taken up by polypeptide chains that consists of alternating strands linked by hydrogen bonds. The alternating strands together form a sheet that is frequently twisted. One of the secondary structural elements characteristic of proteins.
flat sections of a polypeptide due to hydrogen bonding between regions that run antiparallel to each other. It is a type of protein secondary structure.
A pleated section within a protein structure.
A portion of a protein structure which forms a sheet like structure due to how it hydrogen bonds to and adjacent protein strand
A robust protein sheet formed in the PrPsc Prion by the joining up of a number of Beta Strands, providing a very robust structure for the Prion and making it nearly indestructible.
A three-dimensional structure of a protein that takes on a flat, pleated appearance.
The β sheet (also β-pleated sheet) is the second form of regular secondary structure in proteins — the first is the alpha helix — consisting of beta strands connected laterally by three or more hydrogen bonds, forming a generally twisted, pleated sheet. A beta strand (also β-strand) is a stretch of amino acids typically 5–10 amino acids long whose peptide backbones are almost fully extended. The association of beta sheets has been implicated in the formation of protein aggregates and fibrils observed in many human diseases, including Alzheimer's disease and mad cow disease.