Open AccessX‐Ray and Neutron Small‐Angle Scattering Studies of the Complex between Protein S1 and the 30‐S Ribosomal Subunit
Author(s) -
LAUGHREA Michael,
ENGELMAN Donald M.,
MOORE Peter B.
Publication year - 1978
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1978.tb12268.x
Subject(s) - protein subunit , ribosomal protein , radius of gyration , ribosomal rna , eukaryotic large ribosomal subunit , crystallography , scattering , ribosome , chemistry , physics , biochemistry , nuclear magnetic resonance , optics , 18s ribosomal rna , rna , gene , polymer
X‐ray and neutron solution scattering experiments have been done to investigate the influence of the binding of ribosomal protein S1 on the conformation of the 30‐S ribosomal subunit of Escherichia coli . The following conclusions were made.1 The alterations (if any) in conformation of the non‐S1 parts of the 30‐S subunit induced by S1 binding are too small to be detected (< 0.1 nm change in radius of gyration). 2 The center of gravity of protein S1 bound to the 30‐S subunit is quite far from the center of gravity of the particle (≅ 7.5 nm).