Unknown

Dataset Information

0

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


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

Similar Datasets

| S-EPMC3979677 | biostudies-literature
| S-EPMC9992928 | biostudies-literature
| S-EPMC7880565 | biostudies-literature
| S-EPMC11001404 | biostudies-literature
| S-EPMC1161527 | biostudies-other
| S-EPMC4585563 | biostudies-literature
| S-EPMC4974648 | biostudies-literature
| S-EPMC3124082 | biostudies-literature
2011-11-23 | GSE33773 | GEO
| S-EPMC6447237 | biostudies-literature