title: Mass spectrometry of hydrogen/deuterium exchange in 70S ribosomal proteins from E. coli.
abstract: The 70S ribosome from Escherichia coli is a supermacro complex (MW: 2.7MDa) comprising three RNA molecules and more than 50 proteins. We have for the first time successfully analyzed the flexibility of 70S ribosomal proteins in solution by detecting the hydrogen/deuterium exchange with mass spectrometry. Based on the deuterium incorporation map of the X-ray structure obtained at the time of each exchange, we demonstrate the structure-flexibility-function relationship of ribosome focusing on the deuterium incorporation of the proteins binding ligands (tRNA, mRNA, and elongation factor) and the relation with structural assembly processes.
authors.affiliation: Center for Quantum Life Sciences, Graduate School of Science, Hiroshima University, Higashi-Hiroshima 739-8526, Japan. tyamamot@hiroshima-u.ac.jp
authors.forename: Tatsuya
authors.initials: T
authors.lastname: Yamamoto
authors.forename: Shunsuke
authors.initials: S
authors.lastname: Izumi
authors.forename: Kunihiko
authors.initials: K
authors.lastname: Gekko
mesh_terms: D041961:Deuterium Exchange Measurement; D004926:Escherichia coli / Q000737:chemistry*; D008958:Models, Molecular; D012269:Ribosomal Proteins / Q000737:chemistry*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D012269:Ribosomal Proteins