L11 domain rearrangement upon binding to RNA and thiostrepton studied by NMR spectroscopy
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چکیده
منابع مشابه
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 highly conserved complex between the ribosomal protein L11 and the GTPase region of 23S rRNA. The ...
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ژورنال
عنوان ژورنال: Nucleic Acids Research
سال: 2006
ISSN: 1362-4962,0305-1048
DOI: 10.1093/nar/gkl1066