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Turns

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Circular Dichroism and the Conformational Analysis of Biomolecules

Abstract

β and γ turns have been recognized as forming an important group of regular or ordered secondary structures of proteins. β turns are sites where the polypeptide chain reverses its overall direction. Using a hard-sphere model-building technique, Venkatachalam (1968) explored favorable H-bonded conformations of the three consecutive amide units of β turns (see Chou and Fasman, 1977, and references therein). The x-ray structural analysis of an increasing number of proteins (Richardson, 1981; Kabsch and Sander, 1983) has revealed that β turns are common in proteins, accounting for 25–30% of the residues of the total molecule. Lewis et al. (1973) found that about one-fourth of β turns do not possess the H-bond stipulated by Venkatachalam.

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  1. Department of Organic Chemistry, Eötvös University, H-1518, Budapest 112, Hungary

    András Perczel & Miklós Hollósi

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  1. András Perczel
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  1. Department of Biochemistry, Brandeis University, 02254-9110, Waltham, Massachusetts, USA

    Gerald D. Fasman

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Perczel, A., Hollósi, M. (1996). Turns. In: Fasman, G.D. (eds) Circular Dichroism and the Conformational Analysis of Biomolecules. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-2508-7_9

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