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Spin-label study of the conformational states of polypeptide models of histones

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Abstract

The conformational states of the regular polypeptides (Gly-Lys-Gly)n, (Ala-Orn-Gly)n, and (Ala-Orn-Ala)n have been studied by the spin-label method. Their behavior in solutions of guanidine hydrochloride and urea and in solutions of salts of bivalent metals does not contradict the presence of an extended levohelical conformation in their polypeptide chains. In CaCl2 (5 N) solutions the polypeptides exhibit aggregation properties. A study of the behavior of the poly peptide at these temperatures has shown that with a rise in temperature there is a monotonic change in the structures of the polypeptide chains that is characteristic for a conformation of the polyproline-II type. Differences have been observed in the behavior of glycine-and alanine-containing polypeptides in the presence of sodium dodecyl sulfate with a change in the temperature.

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Authors
  1. R. R. Kamilova
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  2. V. K. Burichenko
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Additional information

V. I. Nikitin Institute of Chemistry of the Academy of Sciences of the Tadzhik SSR, Dushanbe. Translated from Khimiya Prirodnykh Soedinenii, No. 2, pp. 218–222, March–April, 1986.

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Kamilova, R.R., Burichenko, V.K. Spin-label study of the conformational states of polypeptide models of histones. Chem Nat Compd 22, 203–207 (1986). https://doi.org/10.1007/BF00574740

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  • DOI: https://doi.org/10.1007/BF00574740

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