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Sensitivity-enhanced Four-dimensional amide-amide correlation NMR experiments for sequential assignment of proline-rich disordered proteins.

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Wong,  L. E.
Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Maier,  J.
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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Griesinger,  C.
Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Supplementary Material (public)

2555267_Suppl_1.pdf
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2555267_Suppl_2.txt
(Supplementary material), 10KB

2555267_Suppl_3.txt
(Supplementary material), 7KB

Citation

Wong, L. E., Maier, J., Wienands, J., Becker, S., & Griesinger, C. (2018). Sensitivity-enhanced Four-dimensional amide-amide correlation NMR experiments for sequential assignment of proline-rich disordered proteins. Journal of the American Chemical Society, 140(10), 3518-3522. doi:10.1021/jacs.8b00215.


Cite as: http://hdl.handle.net/21.11116/0000-0000-BA21-9
Abstract
Proline is prevalent in intrinsically disordered proteins (IDPs). NMR assignment of proline-rich IDPs is a challenge due to low dispersion of chemical shifts. We propose here new sensitivity-enhanced 4D NMR experiments that correlate two pairs of amide resonances that are either consecutive (NHi-1, NHi) or flanking a proline at position i-1 (NHi-2, NHi). The maximum two-fold enhancement of sensitivity is achieved by employing two coherence order-selective (COS) transfers incorporated unconventionally into the pulse sequence. Each COS transfer confers an enhancement over amplitude-modulated transfer by a factor of √2 specifically when transverse relaxation is slow. The experiments connect amide resonances over a long fragment of sequence interspersed with proline. When this method was applied to the proline-rich region of B cell adaptor protein SLP-65 (pH 6.0) and α-synuclein (pH 7.4), which contain a total of 52 and 5 prolines, respectively, 99 % and 92 % of their non-prolyl amide resonances have been successfully assigned, demonstrating its robustness to address the assignment problem in large proline-rich IDPs.