Open AccessGeometry of the Protein S4 from Escherichia coli Ribosomes
Author(s) -
PARADIES H. Hasko,
FRANZ Alfred
Publication year - 1976
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1976.tb10627.x
Subject(s) - radius of gyration , gyration , ribosome , scattering , radius , small angle x ray scattering , small angle scattering , sedimentation equilibrium , crystallography , escherichia coli , molecular physics , chemistry , random coil , cross section (physics) , particle (ecology) , physics , geometry , ultracentrifuge , nuclear magnetic resonance , circular dichroism , optics , mathematics , polymer , rna , biology , biochemistry , computer science , gene , computer security , ecology , quantum mechanics
The shape of protein S4 from Escherichia coli ribosomes in solution was determined by hydrodynamic methods and low‐angle X‐ray scattering. The molecular weight of 24000 determined by low‐angle X‐ray scattering is within 3% of that found by sedimentation equilibrium analysis and 8% of that determined by amino acid sequence work. The radius of gyration of 3.36 nm. the radius of gyration of the cross section of 0.41 nm and the hydrodynamic studies revealed that protein S4 is not spherical, but rather has a markedly extended shape. Calculations of different conformations, e.g. random coil, based on the parameters evaluated from hydrodynamic methods, revealed a rod‐like structure of S4 with a length of 14 nm and a diameter of 1 nm. This is supported by a model of an equivalent scattering particle of uniform density based on all parameters obtained in this study.