L11 domain rearrangement upon binding to RNA and thiostrepton studied by NMR spectroscopy

@inproceedings{Jonker2007L11DR,
  title={L11 domain rearrangement upon binding to RNA and thiostrepton studied by NMR spectroscopy},
  author={Hendrik R. A. Jonker and Serge Ilin and Sebastian K. Grimm and Jens W{\"o}hnert and Harald Schwalbe},
  booktitle={Nucleic acids research},
  year={2007}
}
Ribosomal proteins are assumed to stabilize specific RNA structures and promote compact folding of the large rRNA. The conformational dynamics of the protein between the bound and unbound state play an important role in the binding process. We have studied those dynamical changes in detail for the highly conserved complex between the ribosomal protein L11… CONTINUE READING