A - Papers appearing in refereed journals
Tamas, L., Greenfield, J., Halford, N. G., Tatham, A. S. and Shewry, P. R. 1994. A beta-turn rich barley seed protein is correctly folded in escherichia-coli. Protein Expression and Purification. 5 (4), pp. 357-363.
|Authors||Tamas, L., Greenfield, J., Halford, N. G., Tatham, A. S. and Shewry, P. R.|
Wild-type and cysteine-containing mutant C hordeins from barley were expressed in Escherichia coli at high levels (greater-than-or-equal-to 30 mg/liter). N-terminal sequence analysis, SDS-PAGE, RP-HPLC, cd spectroscopy, and small angle X-ray scattering demonstrated that their physicochemical properties were similar to those of C hordeins isolated from barley grain. This indicates that the expressed proteins were correctly folded. The cysteine-containing mutant showed evidence of polymer formation in E. coli, nonreduced preparations of the protein showing the presence of polymers that were replaced by a single protein when a reducing agent was added. (C) 1994 Academic Press, Inc.
|Keywords||wheat gluten proteins; c-hordein; saccharomyces-cerevisiae; Storage; Proteins; expression vectors; Yeast; gliadin; subunit; Genes|
|Year of Publication||1994|
|Journal||Protein Expression and Purification|
|Journal citation||5 (4), pp. 357-363|
|Digital Object Identifier (DOI)||doi:10.1006/prep.1994.1052|
|Open access||Published as non-open access|
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