Small-angle X-ray-scattering studies of the C hordeins of barley (Hordeum vulgare).
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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.
SUBMITTER: I'Anson KJ
PROVIDER: S-EPMC1133141 | biostudies-other | 1992 Oct
REPOSITORIES: biostudies-other
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