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Mass spectrometry of intact ribosomes
Author(s) -
Videler Hortense,
Ilag Leopold L.,
McKay Adam R.C.,
Hanson Charlotte L.,
Robinson Carol V.
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.12.003
Subject(s) - ribosome , mass spectrometry , dissociation (chemistry) , chemistry , biophysics , eukaryotic ribosome , yeast , elongation , biochemistry , nanotechnology , biology , rna , chromatography , materials science , organic chemistry , ultimate tensile strength , metallurgy , gene
The ability to maintain intact ribosomes in the mass spectrometer has enabled research into their changes in conformation and interactions. In the mass spectrometer, it is possible to induce dissociation of proteins from the intact ribosome and, in conjunction with atomic structures, to understand the factors governing their release. We have applied this knowledge to interpret the structural basis for release of proteins from ribosomes for which no high resolution structures are available, such as complexes with elongation factor G and ribosomes from yeast. We also describe how improvements in technology and understanding have widened the scope of our research and lead to dramatic improvements in quality and information available from spectra of intact ribosomes.