About: Beta turn

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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. 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 Cα atoms of residues i and i+3.

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  • Eine β-Schleife (auch β-Kehre, englisch β-Turn, seltener Haarnadelschleife oder Haarnadelkehre) ist ein Sekundärstrukturmotiv von Peptiden und Proteinen. Sie kommt häufiger vor als die ähnlichen , oder γ-Schleifen. (de)
  • 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. 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 Cα 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. (en)
  • β-转角是是多肽链中常见的二级结构。 (zh)
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  • Eine β-Schleife (auch β-Kehre, englisch β-Turn, seltener Haarnadelschleife oder Haarnadelkehre) ist ein Sekundärstrukturmotiv von Peptiden und Proteinen. Sie kommt häufiger vor als die ähnlichen , oder γ-Schleifen. (de)
  • β-转角是是多肽链中常见的二级结构。 (zh)
  • 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. 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 Cα atoms of residues i and i+3. (en)
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  • Β-Schleife (de)
  • Beta turn (en)
  • Β-转角 (zh)
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