Beta bulge

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A beta bulge is a localized disruption of the regular hydrogen bonding of a beta sheet, usually by inserting a residue with helical dihedral angles into one or both H-bonded β-strands.

[edit] Types

β-bulges can be grouped according to their length of the disruption, the number of residues inserted into each strand, whether the disrupted β-strands are parallel or antiparallel and by their dihedral angles (which controls the placement of their side chains).

[edit] Effects on structure

At the level of the backbone structure, β-bulges can cause a simple aneurysm of the β-sheet, e.g., the bulge in the long β-hairpin of ribonuclease A (residues 88-91). A β-bulge can also cause a β-sheet to fold over and cross itself, e.g., when two residues with left-handed and right-handed α-helical dihedral angles are inserted opposite to each other in a β-hairpin, as occurs at Met9 and Asn16 in pseudoazurin (PDB accession code 1PAZ).

[edit] References

  • Richardson JS, Getzoff ED and Richardson DC. (1978) "The β-bulge: A common small unit of nonrepetitive protein structure", Proc. Natl. Acad. Sci. USA, 75, 2574-2578.
  • Richardson JS. (1981) "The anatomy and taxonomy of protein structure", Adv. Protein Chem., 34, 167-339.
  • Chan AWE, Hutchinson EG, Harris D and Thornton JM. (1993) "Identification, classification, and analysis of beta-bulges in proteins", Protein Sci., 2, 1574-1590.


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→