alpha helix

It is thought to have at least two alpha helices.

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

An alpha helix is created by alternating groups of atoms.

If two or more alpha helices come together, they become a tertiary structure.

The basic domain forms an extended alpha helix in the structure.

This protein domain is known to contain one short alpha helix.

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

The central region contains two alpha helices and four beta strands.

The other domains form a super-helix of short alpha helices.

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

This protein contains 10 beta strands and 2 alpha helices.

This domain is composed of four alpha helices arranged in a bundle.

They are structurally similar to one another, both having 5 transmembrane alpha helices.

The domain consists of three alpha helices separated by loops.

Regarding its structure, it contains 2 alpha helices and 7 beta strands.

Secondary structure includes the formation of alpha helices and 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.

The transmembrane of tetherin is predicted to be a single alpha helix.

There are two transmembrane domains, each with six spans of alpha helices.

The alpha helices of the β subunit form a barrel.

The head consists of the eight alpha helices.

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

It has eight alpha helices and a hydrophobic core.

An alpha helix (α-helix) is a twisted part of a protein.