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Small-angle X-ray scattering investigations on seed proteins

✍ Scribed by Plietz, P. ;Damaschun, G. ;Schwenke, K. D. ;Schlesier, B.

Publisher
John Wiley and Sons
Year
1986
Tongue
English
Weight
601 KB
Volume
30
Category
Article
ISSN
0027-769X

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✦ Synopsis

The 1 IS globulins from sunflower and rape seeds as well as from broad beans were investigated by small-angleX-rayscattering.Theproteinshavemolarmassesof3.0 x lo5 g/Mol,3.0 x 10' g/Moland3.5 x 105g/Mol, respectively. The shapes of the molecules are nearly spherical. They consist in each case of 6 similarly structured subunits, arranged in the molecule as a trigonal antiprism in the dihedral point group symmetry 32. This structure seems to be typical for all 11s globulins from dicotyledons.

The 7s globulin from french beans has a molar mass of 1.45 x lo5 g/Mol. The shape of the molpcule is disk-like. The molecule consists of three subunits separated by deep clefts filled with solvent. The molecule has a three-fold symmetry axis perpendicular to the plane of the disk.

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Abstraet--Methylvinylpyridine-butadiene copolymers vulcanized by various a, oJ dibromo-alkanes were investigated by X-ray small angle scattering. In these systems, employing the Hosemann-Joerchel analysis, only one cluster dimension of about 45 A, has been found with a polydispersity not exceeding 3