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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). 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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-4B01-7 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-80C1-1
Genre: Journal Article

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 Creators:
Yao, X.1, Author              
Becker, S.2, Author              
Zweckstetter, M.1, Author              
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for Biophysical Chemistry, Max Planck Society, ou_578571              
2Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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Free keywords: NMR; Intrinsically disordered protein; Assignment;Alpha-synuclein; APSY; Solvent exchange
 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.

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Language(s): eng - English
 Dates: 2014-11-042014-12
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1007/s10858-014-9872-9
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Title: Journal of Biomolecular NMR
Source Genre: Journal
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Pages: - Volume / Issue: 60 (4) Sequence Number: - Start / End Page: 231 - 240 Identifier: -