The binding site is between beta sheets eight and nine.

Algorithms do not agree on any location for a beta sheet structure.

Many proteins may adopt a beta sheet as part of their secondary structure.

As can be seen in the image, the protein is made of helices and beta sheets.

This structure has a number of alpha helices and beta sheets.

The most common examples are the alpha helix, beta sheet and turns.

The most common secondary structures are alpha helices and beta sheets.

Each module contains two small beta sheets and three disulfide bonds.

Each monomer is a 127-residue polypeptide rich in beta sheet structure.

This protein domain contains both alpha helices and beta sheets.

The secondary structure of this domain is 5% alpha helical and 46% beta sheet.

Secondary structure includes the formation of alpha helices and beta sheets.

Beta-strand is a structural unit of protein beta sheets.

The C-terminal domain is made of two alpha helices and one beta sheet.

The protein is composed of alpha helices and beta sheets to form two domains.

In particular, the beta sheets are arranged in an antiparallel formation.

Two common folding patterns seen in proteins are the alpha helix and beta sheets.

Protein structure like beta sheet shows positive Cotton Effect.

Each beta sheet has five strands, arranged in a 32145 order, with the second strand being antiparallel to the rest.

These repeats typically form a four stranded anti-parallel beta sheet or blade.

The sequence consists mostly of alpha helicies but beta sheets are not absent.

In one study, beta sheet composition only decreased by 13% with calcium ions present compared to 19% when absent.

This forms a beta sheet flanked by a layer of alpha helices on each side.

The domain comprises a six stranded beta sheet of the Rossman fold.

They are typically composed of 4-5 alpha helices and a three-stranded beta sheet.