beta-type structures

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Various secondary structural regions of proteins formed from beta-strands (as opposed to alpha-helical regions). Beta-strands are stretches of amino acids (5–10 aa) in which the peptide backbone is almost fully extended. Beta-arches involve two adjacent antiparallel beta-strands from different sheets, joined by a coiled region usually forming a beta-sandwich. In beta-barrels a series of (typically amphipathic) beta sheets are arranged around a central pore as in voltage-gated ion channels. Beta hairpins are antiparallel beta strands lying adjacent in a sheet. A beta-helix is a large right-handed coil (or superhelix) containing two or three beta-sheets. Beta pleated sheets (beta-sheets) are formed from multiple strands—parallel, antiparallel, or a mixture—linked by interchain hydrogen bonds between peptide carboxyl and amino groups.

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