Beta hairpin

From Wikipedia, the free encyclopedia

Cartoon representation of a β-hairpin
Cartoon representation of a β-hairpin

The beta hairpin (or beta-beta unit) structural motif is the simplest protein motif involving two beta strands that look like a hairpin. 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.

Researchers such as Francisco Blanco et al. have used protein NMR to show that beta-hairpins can be formed from isolated short peptides in aqueous solution, suggesting that hairpins could form nucleation sites for protein folding.[1]

[edit] References

  1. ^ Blanco FJ, Rivas G, Serrano L. (1994). A short linear peptide that folds into a native stable beta-hairpin in aqueous solution. Nat Struct Biol 1(9):584-90. PMID 7634098


Protein secondary structure
Helices: α-helix | 310 helix | π-helix | β-helix | Polyproline helix | Collagen helix
Extended: β-strand | Turn | Beta hairpin | Beta bulge | α-strand
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→