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  Model-free analysis of protein backbone motion from residual dipolar couplings

Peti, W., Meiler, J., Bruschweiler, R., & Griesinger, C. (2002). Model-free analysis of protein backbone motion from residual dipolar couplings. Journal of the American Chemical Society, 124(20), 5822-5833. Retrieved from http://pubs.acs.org/doi/pdfplus/10.1021/ja011883c.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-F3BE-6 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-E552-8
Genre: Journal Article

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Peti, W.1, Author
Meiler, J., Author
Bruschweiler, R., Author
Griesinger, C.2, Author              
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2Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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 Abstract: On the basis of the measurement of NH residual dipolar couplings (RDCs) in 11 different alignment media, an RDC-based order parameter is derived for each residue in the protein ubiquitin. Dipolar couplings are motionally averaged in the picosecond to millisecond time range and, therefore, reflect motion slower than the inverse overall tumbling correlation time of the protein. It is found that there is considerable motion that is slower than the correlation time and could not be detected with previous NMR methodology. Amplitudes and anisotropies of the motion can be derived from the model-free analysis. The method can be applied provided that at least five sufficiently different alignment media can be found for the biomolecule under investigation.

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Language(s): eng - English
 Dates: 2002-05-22
 Publication Status: Published in print
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 Rev. Method: Peer
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Title: Journal of the American Chemical Society
Source Genre: Journal
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Pages: - Volume / Issue: 124 (20) Sequence Number: - Start / End Page: 5822 - 5833 Identifier: -