Heteronuclear NMR investigations of dynamic regions of intact Escherichia coli ribosomes.

Journal article

15N-(1)H NMR spectroscopy has been used to probe the dynamic properties of uniformly (15)N labeled Escherichia coli ribosomes. Despite the high molecular weight of the complex ( approximately 2.3 MDa), [(1)H-(15)N] heteronuclear single-quantum correlation spectra contain approximately 100 well resolved resonances, the majority of which arise from two of the four C-terminal domains of the stalk proteins, L7/L12. Heteronuclear pulse-field gradient NMR experiments show that the resonances arise ...

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Authors: Christodoulou, J; Larsson, G; Fucini, P; Connell, SR; Pertinhez, T

• Publication status: Published
• Journal: Proceedings of the National Academy of Sciences of the United States of America
• Volume: 101
• Issue: 30
• Pages: 10949-10954
• Publication date: 2004-07-01
• DOI: 10.1073/pnas.0400928101
• EISSN: 1091-6490
• ISSN: 0027-8424
• Language: English
• Keywords: Escherichia coli; Ribosomes; Models, Molecular; Ribosomal Proteins; Magnetic Resonance Spectroscopy; Peptide Elongation Factor G; Quantum Theory; Nitrogen Isotopes; Escherichia coli Proteins; Protein Conformation