Backbone assignment for minimal protein amounts of low structural homogeneity 
in the absence of deuteration.

Xiang, S.; Biernat, J.; Mandelkow, E.; Becker, S.; Linser, R.

doi:10.1039/C5CC09160H

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Backbone assignment for minimal protein amounts of low structural homogeneity in the absence of deuteration.

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Xiang, S.
Research Group of Solid-State NMR-2, 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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Linser, R.
Research Group of Solid-State NMR-2, MPI for Biophysical Chemistry, Max Planck Society;

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Citation

Xiang, S., Biernat, J., Mandelkow, E., Becker, S., & Linser, R. (2016). Backbone assignment for minimal protein amounts of low structural homogeneity in the absence of deuteration. Chemical Communications, 52(21), 4002-4005. doi:10.1039/C5CC09160H.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0029-60E0-7

Abstract

NMR characterization of many proteins is limited by low expression, hurdles for deuteration, and poor sample homogeneity. We introduce a set of high-dimensionality proton-detected experiments developed for unambiguous resonance assignments of such proteins, which we could successfully apply to a 1-mg amount of non-deuterated Tau paired helical filaments.