Open AccessSmall‐Angle X‐Ray Scattering Studies on Virus‐Like Protein Particles Derived from Bacteriophage fr
Author(s) -
Zipper Peter,
Schubert Dieter,
Vogt Jürgen
Publication year - 1973
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1973.tb02914.x
Subject(s) - radius of gyration , radius , ultracentrifuge , bacteriophage , crystallography , scattering , chemistry , physics , chromatography , optics , polymer , escherichia coli , biochemistry , computer security , organic chemistry , computer science , gene
Small‐angle X‐ray scattering and analytical ultracentrifugation were applied to solutions of virus‐like protein particles prepared from bacteriophage fr by alkaline degradation of the phage (artificial top component) as well as by self‐assembly of the monomeric protein subunits in the absence of nucleic acid. The artificial top component sediments with 42 S, while the reaggregated protein particles were found to sediment on the average with 45.4 S. The radial dimensions of the artificial top component are practically identical to those of the protein shell of the virus, the inner radius being 10.6 nm and the outer radius being 13.2 nm. The same outer radius was obtained also for the reaggregated protein particles, except for one out of four samples which showed slight remainders of multishells on the outer surface. For the other samples, the molecular weight was found to be higher than that of the artificial top component by about 8%, whereas the radius of gyration was smaller by about 3.6%. From these results and from the radial net electron density distribution, it is concluded that the reaggregated protein particles contain on the average 14.4 additional protein subunits located in their interior.