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

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 h...

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Bibliografiska uppgifter
Huvudupphovsmän: Jonker, Hendrik R. A., Ilin, Serge, Grimm, S. Kaspar, Wöhnert, Jens, Schwalbe, Harald
Materialtyp: Artigo
Språk:Inglês
Publicerad: Oxford University Press 2007
Ämnen:
Structural Biology
Länkar:https://ncbi.nlm.nih.gov/pmc/articles/PMC1802607/
https://ncbi.nlm.nih.gov/pubmed/17169991
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/nar/gkl1066
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