A six-dimensional alpha proton detection-based APSY experiment for backbone assignment of intrinsically disordered proteins
2014 | journal article. A publication with affiliation to the University of Göttingen.
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A six-dimensional alpha proton detection-based APSY experiment for backbone assignment of intrinsically disordered proteins
Yao, X.; Becker, S. & Zweckstetter, M. (2014)
Journal of Biomolecular NMR, 60(4) pp. 231-240. DOI: https://doi.org/10.1007/s10858-014-9872-9
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Details
- Authors
- Yao, Xuejun; Becker, Stefan; Zweckstetter, Markus
- 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, H-alpha(i - 1), C-alpha(i - 1), C'(i - 1), N(i), C-alpha(i) and H-alpha(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.
- Issue Date
- 2014
- Status
- published
- Publisher
- Springer
- Journal
- Journal of Biomolecular NMR
- ISSN
- 1573-5001; 0925-2738
- Sponsor
- DFG [ZW71/3-2, ZW71/7-1]