抄録
The 70S ribosome of Escherichia coli, which plays a central role in peptide synthesis in cells, is a super-macro complex (2.7 MDa) comprising three RNA molecules and more than 50 proteins. We succeeded in measuring the hydrogen/deuterium exchange of 55 ribosomal proteins by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The results revealed the structural flexibility and solvent accessibility of individual proteins, and provided useful information on the structure-flexibility-function relationships of 70S ribosome.
