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Heteronuclear NMR investigations of dynamic regions of intact Escherichia coli ribosomes.

Abstract:

15N-(1)H NMR spectroscopy has been used to probe the dynamic properties of uniformly (15)N labeled Escherichia coli ribosomes. Despite the high molecular weight of the complex ( approximately 2.3 MDa), [(1)H-(15)N] heteronuclear single-quantum correlation spectra contain approximately 100 well resolved resonances, the majority of which arise from two of the four C-terminal domains of the stalk proteins, L7/L12. Heteronuclear pulse-field gradient NMR experiments show that the resonances arise ...

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Publication status:
Published

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Publisher copy:
10.1073/pnas.0400928101

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Journal:
Proceedings of the National Academy of Sciences of the United States of America
Volume:
101
Issue:
30
Pages:
10949-10954
Publication date:
2004-07-05
DOI:
EISSN:
1091-6490
ISSN:
0027-8424
URN:
uuid:4fa0c29a-dc5d-434b-8675-7b901b05f529
Source identifiers:
59264
Local pid:
pubs:59264

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