A - Papers appearing in refereed journals
Halford, N. G., Tatham, A. S., Sui, E., Daroda, L., Dreyer, T. and Shewry, P. R. 1992. Identification of a novel beta-turn-rich repeat motif in the D hordeins of barley. Biochimica Et Biophysica Acta. 1122 (2), pp. 118-122.
|Authors||Halford, N. G., Tatham, A. S., Sui, E., Daroda, L., Dreyer, T. and Shewry, P. R.|
The amino acid sequence of the C-terminal part of a barley D hordein seed protein was deduced from the nucleotide sequence of a partial cDNA. It showed high homology with the HMW glutenin subunits of wheat, both proteins consisting predominately of repeated sequences. Whereas the wheat repeats are based on tri-, hexa- and nonapeptides that are rich in glycine, proline and glutamine, the D hordein also contains eleven copies of a novel unrelated motif: Thr-Thr-Val-Ser. The repeated sequences in the wheat glutenin subunits have been demonstrated to form an unusual spiral supersecondary structure based on beta-turns. Conformational analysis of the Thr-Thr-Val-Ser motif by secondary structure prediction and by circular dichroism spectroscopy of an 18 residue synthetic peptide demonstrates that it also forms beta-turns. Thus, D hordein may also have a spiral structure like that of HMW glutenin, despite the presence of a different repeat motif. This conservation of protein conformation in D hordein and the wheat glutenin subunits may indicate a structural role, perhaps in packing of the proteins within the protein bodies of the developing grain.
|Keywords||seed protein; repetitive sequence; beta-turn; beta-spiral; supersecondary structure; protein conformation; hmw glutenin subunits; Wheat Gluten; amino-acids; Proteins; expression; sequence; bends|
|Year of Publication||1992|
|Journal||Biochimica Et Biophysica Acta|
|Journal citation||1122 (2), pp. 118-122|
|Digital Object Identifier (DOI)||doi:10.1016/0167-4838(92)90313-3|
|Open access||Published as non-open access|
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