A combination of c.d. spectroscopy and computer prediction is used to show that C hordein has an unusual secondary structure with an absence of alpha-helix and beta-sheet, but the presence of regularly repeated beta-turns. This is associated with a repetitive primary structure based mainly on blocks of eight residues. Similar spectral changes occurred when the protein was heated from 6 to 86 degrees C in aq. 70% (v/v) ethanol or dissolved in increasing concentrations (50-100%, v/v) of trifluoroethanol in water. The studies indicated that the conformation is stabilized by strong hydrophobic interactions and by extensive hydrogen-bonding.
Research Article| March 01 1985
A conformational study of a glutamine- and proline-rich cereal seed protein, C hordein
Biochem J (1985) 226 (2): 557–562.
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A S Tatham, A F Drake, P R Shewry; A conformational study of a glutamine- and proline-rich cereal seed protein, C hordein. Biochem J 1 March 1985; 226 (2): 557–562. doi: https://doi.org/10.1042/bj2260557
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