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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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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-E2AF-F Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-DBBC-7
Genre: Journal Article

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319647.pdf (Publisher version), 0B
 
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 Creators:
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: Published in print
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 Table of Contents: -
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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: -