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The native conformation of the human VDAC1 N terminus.

MPS-Authors
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Schneider,  R.
Research Group of Solid-State NMR, MPI for biophysical chemistry, Max Planck Society;

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Etzkorn,  M.
Research Group of Solid-State NMR, MPI for biophysical chemistry, Max Planck Society;

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

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

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Lange,  A.
Research Group of Solid-State NMR, MPI for biophysical chemistry, Max Planck Society;

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Citation

Schneider, R., Etzkorn, M., Giller, K., Daebel, V., Eisfeld, J., Zweckstetter, M., et al. (2010). The native conformation of the human VDAC1 N terminus. Angewandte Chemie - International Edition, 49(10), 1882-1885. doi:10.1002/anie.200906241.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0012-D62F-1
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