Quantitative determination of the conformational properties of partially folded 
and intrinsically disordered proteins using NMR dipolar couplings.

Jensen, M. R.; Markwick, P. R.; Meier, S.; Griesinger, C.; Zweckstetter, M.; Grzesiek, S.; Bernado, P.; Blackledge, M.

doi:10.1016/j.str.2009.08.001

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Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings.

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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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Citation

Jensen, M. R., Markwick, P. R., Meier, S., Griesinger, C., Zweckstetter, M., Grzesiek, S., et al. (2009). Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings. Structure, 17(9), 1169-1185. doi:10.1016/j.str.2009.08.001.

Cite as: https://hdl.handle.net/11858/00-001M-0000-000F-9EA6-1

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