Beta hairpin
From Wikipedia, the free encyclopedia
The beta hairpin (or beta-beta unit) structural motif is the simplest protein motif involving two beta strands. The motif consists of two strands that are adjacent in primary sequence oriented in an antiparallel arrangement (where the N-terminus of one sheet is adjacent to the C-terminus of the next) and linked by a short loop of two to five amino acids. Beta hairpins can occur in isolation or as part of a series of hydrogen bonded strands that collectively comprise a beta sheet.
| Protein secondary structure | ||
|---|---|---|
| Helices: | α-helix | 310 helix | π-helix | β-helix | Polyproline helix | Collagen helix | |
| Extended: | β-strand | Turn | Beta hairpin | Beta bulge | |
| Supersecondary: | Coiled coil | Helix-turn-helix | EF hand | |
| Secondary structure propensities of amino acids | ||
| Helix-favoring: | Methionine | Alanine | Leucine | Glutamic acid | Glutamine | Lysine | |
| Extended-favoring: | Threonine | Isoleucine | Valine | Phenylalanine | Tyrosine | Tryptophan | |
| Disorder-favoring: | Glycine | Serine | Proline | Asparagine | Aspartic acid | |
| No preference: | Cysteine | Histidine | Arginine | |
| ←Primary structure | Tertiary structure→ | |
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