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  Highly populated turn conformations in natively unfolded Tau protein identified from residual dipolar couplings and molecular simulation

Mukrasch, M., Markwick, P., Biernat, J., von Bergen, M., Bernado, P., Griesinger, C., et al. (2007). Highly populated turn conformations in natively unfolded Tau protein identified from residual dipolar couplings and molecular simulation. Journal of the American Chemical Society, 129(16), 5235-5243. Retrieved from http://pubs.acs.org/cgi-bin/article.cgi/jacsat/2007/129/i16/html/ja0690159.html.

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Mukrasch, M.1, Author           
Markwick, P., Author
Biernat, J., Author
von Bergen, M., Author
Bernado, P., Author
Griesinger, C.1, Author           
Mandelkow, E., Author
Zweckstetter, M.2, Author           
Blackledge, M., Author
Affiliations:
1Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              
2Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              

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Language(s): eng - English
 Dates: 2007
 Publication Status: Issued
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Title: Journal of the American Chemical Society
Source Genre: Journal
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Pages: - Volume / Issue: 129 (16) Sequence Number: - Start / End Page: 5235 - 5243 Identifier: -