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Chemical & Structural Biology

NMR studies of the structure and dynamics of the ribosomal protein L11 from Thermotoga maritima.

L11 is highly conserved ribosomal protein and its interaction with the ribosomal RNA segment from 23S subunit is considered to undergo an „induced fit“-conformational adjustment of both the protein and the RNA with respect to their conformations in the unbound state (Leulliot and Varani, 2001; Draper et al., 1996). Furthermore, the conformational dynamics of L11 are thought to play an important role in the binding process.

Comparison of the NMR Spectroscopy Solution Structure of Pyranosyl-RNA and Its Nucleo-delta-peptide Analogue

For all biological systems, nature has chosen ribo- and deoxyribonucleic acids as its genetic building block. In order to understand this selectivity, the structures of the potential alternatives to the natural nucleic acids have to be investigated. We have determined the solution structures of pRNA and Nucleo-d-peptides by NMR spectroscopy. The structures pose important questions about the origin of helicity, stacking and inclination of these oligomers.