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

doi:10.1006/prep.1994.1052

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Article

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

Protein expression and purification - 1 Aug 1994

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

Abstract excerpt

Wild-type and cysteine-containing mutant C hordeins from barley were expressed in Escherichia coli at high levels (> or = 30mg/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....

Topics

Amino Acid Sequence
Base Sequence
Chromatography, High Pressure Liquid
Circular Dichroism
Cysteine
Escherichia coli
Glutens
Hordeum
Molecular Sequence Data
Mutation
Plant Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Folding

Protein Structure, Secondary

Recombinant Proteins

Scattering, Radiation

Sequence Analysis

X-Rays

Source

Open in PubMed

Identifiers

PMID: 7950382
DOI: 10.1006/prep.1994.1052

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7950382-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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