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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Detalles Bibliográficos
Autores principales: Jonker, Hendrik R. A., Ilin, Serge, Grimm, S. Kaspar, Wöhnert, Jens, Schwalbe, Harald
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2007
Materias:
Structural Biology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1802607/
https://www.ncbi.nlm.nih.gov/pubmed/17169991
http://dx.doi.org/10.1093/nar/gkl1066

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1802607/
https://www.ncbi.nlm.nih.gov/pubmed/17169991
http://dx.doi.org/10.1093/nar/gkl1066

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