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.; Mandelkow, E.; Zweckstetter, M.; Blackledge, M.

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

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Mukrasch, M.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Griesinger, C.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Zweckstetter, M.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

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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.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0012-E2AF-F

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