About: 4D Non-uniformly sampled HCBCACON and (1) J(NC alpha)-selective HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins     Goto   Sponge   NotDistinct   Permalink

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Description
  • A pair of 4D NMR experiments for the backbone assignment of disordered proteins is presented. The experiments exploit C-13 direct detection and non-uniform sampling of the indirectly detected dimensions, and provide correlations of the aliphatic proton (H-alpha, and H-beta) and carbon (C-alpha, C-beta) resonance frequencies to the protein backbone. Thus, all the chemical shifts regularly used to map the transient secondary structure motifs in the intrinsically disordered proteins (H-alpha, C-alpha, C-beta, C', and N) can be extracted from each spectrum. Compared to the commonly used assignment strategy based on matching the C-alpha and C-beta chemical shifts, inclusion of the H-alpha and H-beta provides up to three extra resonance frequencies that decrease the chance of ambiguous assignment. The experiments were successfully applied to the original assignment of a 12.8 kDa intrinsically disordered protein having a high content of proline residues (26 %) in the sequence.
  • A pair of 4D NMR experiments for the backbone assignment of disordered proteins is presented. The experiments exploit C-13 direct detection and non-uniform sampling of the indirectly detected dimensions, and provide correlations of the aliphatic proton (H-alpha, and H-beta) and carbon (C-alpha, C-beta) resonance frequencies to the protein backbone. Thus, all the chemical shifts regularly used to map the transient secondary structure motifs in the intrinsically disordered proteins (H-alpha, C-alpha, C-beta, C', and N) can be extracted from each spectrum. Compared to the commonly used assignment strategy based on matching the C-alpha and C-beta chemical shifts, inclusion of the H-alpha and H-beta provides up to three extra resonance frequencies that decrease the chance of ambiguous assignment. The experiments were successfully applied to the original assignment of a 12.8 kDa intrinsically disordered protein having a high content of proline residues (26 %) in the sequence. (en)
Title
  • 4D Non-uniformly sampled HCBCACON and (1) J(NC alpha)-selective HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins
  • 4D Non-uniformly sampled HCBCACON and (1) J(NC alpha)-selective HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins (en)
skos:prefLabel
  • 4D Non-uniformly sampled HCBCACON and (1) J(NC alpha)-selective HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins
  • 4D Non-uniformly sampled HCBCACON and (1) J(NC alpha)-selective HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins (en)
skos:notation
  • RIV/00216224:14740/12:00057624!RIV13-GA0-14740___
http://linked.open...avai/predkladatel
http://linked.open...avai/riv/aktivita
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  • P(ED1.1.00/02.0068), P(GAP206/11/0758)
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  • 2
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  • 183477
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  • RIV/00216224:14740/12:00057624
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  • Intrinsically disordered proteins; Non-uniform sampling; C-13 detection; Chemical shifts; Residual secondary structure; Prolines assignment (en)
http://linked.open.../riv/klicoveSlovo
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  • NL - Nizozemsko
http://linked.open...ontrolniKodProRIV
  • [58D45DE43B9E]
http://linked.open...i/riv/nazevZdroje
  • Journal of Biomolecular NMR
http://linked.open...in/vavai/riv/obor
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  • 53
http://linked.open...iv/tvurceVysledku
  • Nováček, Jiří
  • Sklenář, Vladimír
  • Žídek, Lukáš
  • Chill, Jordan H
  • Haba, Noam Y
http://linked.open...ain/vavai/riv/wos
  • 000305943400007
issn
  • 0925-2738
number of pages
http://bibframe.org/vocab/doi
  • 10.1007/s10858-012-9631-8
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  • 14740
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