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|a 10.1016/j.jmr.2011.10.019
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037 _ _ |a PreJuSER-19969
041 _ _ |a eng
082 _ _ |a 550
084 _ _ |2 WoS
|a Biochemical Research Methods
084 _ _ |2 WoS
|a Physics, Atomic, Molecular & Chemical
084 _ _ |2 WoS
|a Spectroscopy
100 1 _ |0 P:(DE-Juel1)VDB101059
|a Feuerstein, S.
|b 0
|u FZJ
245 _ _ |a iHADAMAC: a complementary tool for sequential resonance assignment of globular and highly disordered protein
260 _ _ |a Amsterdam [u.a.]
|b Elsevier
|c 2012
300 _ _ |a 329 - 334
336 7 _ |a Journal Article
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440 _ 0 |0 9881
|a Journal of Magnetic Resonance
|v 214
|x 1090-7807
500 _ _ |a We thank I. Ayala (IBS Grenoble) for help with the production of the protein samples used for this study, and S. Hoffmann (FZ Julich) for stimulating discussion on the NS5A project. This work has been supported in part by grants from the European Commission (FP7-I3-BIO-NMR contract No. 261862, FP7-ITN-IDPbyNMR contract No. 264257, and FPR-IRG-2008 contract No. 231082), and financial support from ARC to M.J.P. and from CEA to S.F.
520 _ _ |a An experiment, iHADAMAC, is presented that yields information on the amino-acid type of individual residues in a protein by editing the (1)H-(15)N correlations into seven different 2D spectra, each corresponding to a different class of amino-acid types. Amino-acid type discrimination is realized via a Hadamard encoding scheme based on four different spin manipulations as recently introduced in the context of the sequential HADAMAC experiment. Both sequential and intra-residue HADAMAC experiments yield highly complementary information that greatly facilitate resonance assignment of proteins with high frequency degeneracy, as demonstrated here for a 188-residue intrinsically disordered protein fragment of the hepatitis C virus protein NS5A.
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536 _ _ |a IDPBYNMR - High resolution tools to understand the functional role of protein intrinsic disorder (264257)
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|f FP7-PEOPLE-2010-ITN
536 _ _ |a ONCOMIRNA-BIOGENESIS - Biogenesis of Oncogenic MicroRNAs : from the structure of the microRNA processing complexes to the inhibition of the maturation of human oncogenes (231082)
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588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Algorithms
650 _ 2 |2 MeSH
|a Magnetic Resonance Spectroscopy: methods
650 _ 2 |2 MeSH
|a Proteins: chemistry
650 _ 2 |2 MeSH
|a Proteins: ultrastructure
650 _ 2 |2 MeSH
|a Software
650 _ 7 |0 0
|2 NLM Chemicals
|a Proteins
650 _ 7 |2 WoSType
|a J
653 2 0 |2 Author
|a NMR
653 2 0 |2 Author
|a Protein
653 2 0 |2 Author
|a IDP
653 2 0 |2 Author
|a Sequential resonance assignment
653 2 0 |2 Author
|a HADAMAC
700 1 _ |0 P:(DE-HGF)0
|a Plevin, M.J.
|b 1
700 1 _ |0 P:(DE-Juel1)132029
|a Willbold, D.
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700 1 _ |0 P:(DE-HGF)0
|a Brutscher, B.
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773 _ _ |0 PERI:(DE-600)1469665-4
|a 10.1016/j.jmr.2011.10.019
|g Vol. 214, p. 329 - 334
|p 329 - 334
|q 214<329 - 334
|t Journal of magnetic resonance
|v 214
|x 1090-7807
|y 2012
856 7 _ |u http://dx.doi.org/10.1016/j.jmr.2011.10.019
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