Beta turn

β turns (also β-bends, tight turns, reverse turns, Venkatachalam turns) are the most common form of turns—a type of non-regular secondary structure in proteins that cause a change in direction of the polypeptide chain. They are very common motifs in proteins and polypeptides.[1][2][3][4][5][6][7][8][9] Each consists of four amino acid residues (labelled i, i+1, i+2 and i+3). They can be defined in two ways:

  1. By the possession of an intra-main-chain hydrogen bond between the CO of residue i and the NH of residue i+3;
  2. By having a distance of less than 7Å between the atoms of residues i and i+3.

The hydrogen bond criterion is the one most appropriate for everyday use, partly because it gives rise to four distinct categories; the distance criterion gives rise to the same four categories but yields additional turn types.

  1. ^ Venkatachalam, CM (1968). "Stereochemical criteria for polypeptides and proteins. V. Conformation of a system of three linked peptide units" (PDF). Biopolymers. 6 (10): 1425–1436. doi:10.1002/bip.1968.360061006. hdl:2027.42/37819. PMID 5685102. S2CID 5873535.
  2. ^ Lewis, PN; Momany FA (1973). "Chain reversal in proteins". Biochim Biophys Acta. 303 (2): 211–29. doi:10.1016/0005-2795(73)90350-4. PMID 4351002.
  3. ^ Toniolo, C; Benedetti E (1980). "Intramolecularly hydrogen-bonded peptide conformations". CRC Crit Rev Biochem. 9 (1): 1–44. doi:10.3109/10409238009105471. PMID 6254725.
  4. ^ Richardson, JS (1981). "The anatomy and taxonomy of protein structure". Adv Prot Chem. Advances in Protein Chemistry. 34: 167–339. doi:10.1016/S0065-3233(08)60520-3. ISBN 9780120342341. PMID 7020376.
  5. ^ Rose, GD; Gierasch LM (1985). "Turns in peptides and proteins". Adv Prot Chem. Advances in Protein Chemistry. 37: 1–109. doi:10.1016/S0065-3233(08)60063-7. ISBN 9780120342372. PMID 2865874.
  6. ^ Milner-White, EJ; Poet R (1987). "Loops, bulges, turns and hairpins in proteins". Trends Biochem Sci. 12: 189–192. doi:10.1016/0968-0004(87)90091-0.
  7. ^ Wilmot, CM; Thornton JM (1988). "Analysis and prediction of the different types of beta-turn in proteins". J Mol Biol. 203 (1): 221–232. doi:10.1016/0022-2836(88)90103-9. PMID 3184187.
  8. ^ Sibanda, BL; Blundell TL (1989). "Conformation of β-hairpins in protein structures: A systematic classification with applications to modelling by homology, electron density fitting and protein engineering". J Mol Biol. 206 (4): 759–777. doi:10.1016/0022-2836(89)90583-4. PMID 2500530.
  9. ^ Hutchinson, EG; Thornton JM (1994). "A revised set of potentials for β-turn formation in proteins". J Mol Biol. 3 (12): 2207–2216. doi:10.1002/pro.5560031206. PMC 2142776. PMID 7756980.