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A six-dimensional alpha proton detection-based APSY experiment for backbone assignment of intrinsically disordered proteins.

MPS-Authors
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Yao,  X.
Research Group of Protein Structure Determination using NMR, 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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Zweckstetter,  M.
Research Group of Protein Structure Determination using NMR, MPI for Biophysical Chemistry, Max Planck Society;

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2077098_Suppl.pdf
(Supplementary material), 84KB

Citation

Yao, X., Becker, S., & Zweckstetter, M. (2014). A six-dimensional alpha proton detection-based APSY experiment for backbone assignment of intrinsically disordered proteins. Journal of Biomolecular NMR, 60(4), 231-240. doi:10.1007/s10858-014-9872-9.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-4B01-7
Abstract
Sequence specific resonance assignment is the prerequisite for the NMR-based analysis of the conformational ensembles and their underlying dynamics of intrinsically disordered proteins. However, rapid solvent exchange in intrinsically disordered proteins often complicates assignment strategies based on HN-detection. Here we present a six-dimensional alpha proton detection-based automated projection spectroscopy (APSY) experiment for backbone assignment of intrinsically disordered proteins. The 6D HCACONCAH APSY correlates the six different chemical shifts, Halpha(i-1), Calpha(i-1), C'(i-1), N(i), Calpha(i) and Halpha(i). Application to two intrinsically disordered proteins, 140-residue alpha-synuclein and a 352-residue isoform of Tau, demonstrates that the chemical shift information provided by the 6D HCACONCAH APSY allows efficient backbone resonance assignment of intrinsically disordered proteins.