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Conformational changes in the reserve proteins of the cotton plant

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Abstract

A quantitative study of the secondary structures of the 11S and 7S globulins from cotton seeds has been made by the circular dichroism (CD) method. It has been established that the 11S and 7S globulins contain, respectively: 16 and 14% of α-helices; 15% each of β-structures; 18 and 20% of β-bends; and 51% each of irregular sections.

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Authors
  1. Z. S. Yunusova
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  2. G. P. Moiseeva
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  3. I. A. Bolotina
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Additional information

Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Institute of Molecular Biology, Academy of Sciences of the USSR, Moscow. Translated from Khimiya Prirodnykh Soedinenii, No. 3, pp. 355–357, May–June, 1984.

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Yunusova, Z.S., Moiseeva, G.P. & Bolotina, I.A. Conformational changes in the reserve proteins of the cotton plant. Chem Nat Compd 20, 331–333 (1984). https://doi.org/10.1007/BF00575761

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  • DOI: https://doi.org/10.1007/BF00575761

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