Small-angle X-ray-scattering studies of the C hordeins of barley (Hordeum vulgare).
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.
I'Anson
K J
KJ
AFRC Institute of Food Research, Norwich Laboratory, Colney, U.K.
Morris
V J
VJ
Shewry
P R
PR
Tatham
A S
AS
D005983:Glutens; D001467:Hordeum / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry*; D011487:Protein Conformation; D012542:Scattering, Radiation; D012996:Solutions; D014965:X-Rays
D010940:Plant Proteins; D012996:Solutions; D005983:Glutens