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. 1992 Oct 1;287(Pt 1):183–185. doi: 10.1042/bj2870183

Small-angle X-ray-scattering studies of the C hordeins of barley (Hordeum vulgare).

K J I'Anson 1, V J Morris 1, P R Shewry 1, A S Tatham 1
PMCID: PMC1133141  PMID: 1417771

Abstract

Small angle X-ray scattering was used to study the solution conformation of the C hordeins of barley (Hordeum vulgare), a group of proteins whose primary structure consists predominantly of an octapeptide repeat motif. Measurements on the protein in 0.1 M-acetic acid at 25 degrees C are consistent with a model for the protein conformation of a stiff coil, the so-called 'worm-like' chain. The characteristic parameters (the Kuhn statistical segment length and the contour length) of the protein were calculated as 5.11 and 71.5 nm respectively.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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