A beta-turn rich barley seed protein is correctly folded in escherichia-coli

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.

AuthorsTamas, L., Greenfield, J., Halford, N. G., Tatham, A. S. and Shewry, P. R.
Abstract

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.

Keywordswheat gluten proteins; c-hordein; saccharomyces-cerevisiae; Storage; Proteins; expression vectors; Yeast; gliadin; subunit; Genes
Year of Publication1994
JournalProtein Expression And Purification
Journal citation5 (4), pp. 357-363
Digital Object Identifier (DOI)doi:10.1006/prep.1994.1052
Open accessPublished as non-open access
ISSN10465928
1046-5928
Publisher

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