A β-Turn Rich Barley Seed Protein Is Correctly Folded in Escherichia coli

L. Tamas; J. Greenfield; N. G. Halford; A. S. Tatham; P. R. Shewry

doi:10.1006/prep.1994.1052

A β-Turn Rich Barley Seed Protein Is Correctly Folded in Escherichia coli

L. Tamas^*, J. Greenfield, N. G. Halford, A. S. Tatham, P. R. Shewry

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

21 Citations (Scopus)

Abstract

Wild-type and cysteine-containing mutant C hordeins from barley were expressed in Escherichia coli at high levels (≥ 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.

Original language	English
Pages (from-to)	357-363
Number of pages	7
Journal	Protein Expression and Purification
Volume	5
Issue number	4
DOIs	https://doi.org/10.1006/prep.1994.1052
Publication status	Published - Aug 1994
Externally published	Yes

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10.1006/prep.1994.1052

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AU - Shewry, P. R.

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A β-Turn Rich Barley Seed Protein Is Correctly Folded in Escherichia coli

Abstract

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