Abstract
A model treatment ofβ-structural polypeptides with four cysteine residues in a molecule allows us to formulate simple rules of selecting the structures closest to the preferable one and to reveal the most probable positions of SS-bridges. The applicability of this model approach is demonstrated on several examples of peptides with experimentally defined structures.
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Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences. Translated fromZhurnal Strukturnoi Khimii, Vol. 39, No. 3, pp. 529–534, May–June, 1998.
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Golovanov, I.B., Tsygankova, I.G. Topological structures of peptides with cysteine residues. J Struct Chem 39, 432–436 (1998). https://doi.org/10.1007/BF02873654
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DOI: https://doi.org/10.1007/BF02873654