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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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Библиографические подробности
Главные авторы: Jonker, Hendrik R. A., Ilin, Serge, Grimm, S. Kaspar, Wöhnert, Jens, Schwalbe, Harald
Формат: Artigo
Язык:Inglês
Опубликовано: Oxford University Press 2007
Предметы:
Online-ссылка: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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