About: Efficient protocol for backbone and side-chain assignments of large, intrinsically disordered proteins: transient secondary structure analysis of 49.2 kDa microtubule associated protein 2c     Goto   Sponge   NotDistinct   Permalink

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Description
  • Microtubule-associated proteins (MAPs) are abundantly present in axons and dendrites, and have been shown to play crucial role during the neuronal morphogenesis. The period of main dendritic outgrowth and synaptogenesis coincides with high expression levels of one of MAPs, the MAP2c, in rats. The MAP2c is a 49.2 kDa intrinsically disordered protein. To achieve an atomic resolution characterization of such a large protein, we have developed a protocol based on the acquisition of two five-dimensional C-13-directly detected NMR experiments. Our previously published 5D CACONCACO experiment (Novacek et al. in J Biomol NMR 50(1):1-11, 2011) provides the sequential assignment of the backbone resonances, which is not interrupted by the presence of the proline residues in the amino acid sequence. A novel 5D HC(CC-TOCSY)CACON experiment facilitates the assignment of the aliphatic side chain resonances. To streamline the data analysis, we have developed a semi-automated procedure for signal assignments.
  • Microtubule-associated proteins (MAPs) are abundantly present in axons and dendrites, and have been shown to play crucial role during the neuronal morphogenesis. The period of main dendritic outgrowth and synaptogenesis coincides with high expression levels of one of MAPs, the MAP2c, in rats. The MAP2c is a 49.2 kDa intrinsically disordered protein. To achieve an atomic resolution characterization of such a large protein, we have developed a protocol based on the acquisition of two five-dimensional C-13-directly detected NMR experiments. Our previously published 5D CACONCACO experiment (Novacek et al. in J Biomol NMR 50(1):1-11, 2011) provides the sequential assignment of the backbone resonances, which is not interrupted by the presence of the proline residues in the amino acid sequence. A novel 5D HC(CC-TOCSY)CACON experiment facilitates the assignment of the aliphatic side chain resonances. To streamline the data analysis, we have developed a semi-automated procedure for signal assignments. (en)
Title
  • Efficient protocol for backbone and side-chain assignments of large, intrinsically disordered proteins: transient secondary structure analysis of 49.2 kDa microtubule associated protein 2c
  • Efficient protocol for backbone and side-chain assignments of large, intrinsically disordered proteins: transient secondary structure analysis of 49.2 kDa microtubule associated protein 2c (en)
skos:prefLabel
  • Efficient protocol for backbone and side-chain assignments of large, intrinsically disordered proteins: transient secondary structure analysis of 49.2 kDa microtubule associated protein 2c
  • Efficient protocol for backbone and side-chain assignments of large, intrinsically disordered proteins: transient secondary structure analysis of 49.2 kDa microtubule associated protein 2c (en)
skos:notation
  • RIV/00216224:14740/13:00066377!RIV14-MSM-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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  • 4
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  • 72086
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  • RIV/00216224:14740/13:00066377
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  • Nuclear magnetic resonance; Intrinsically disordered proteins; Microtubule-associated protein; Transient secondary structure; C-13 detection (en)
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  • NL - Nizozemsko
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  • [62CE0F4189D4]
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  • Journal of Biomolecular NMR
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  • 56
http://linked.open...iv/tvurceVysledku
  • Dopitová, Radka
  • Janda, Lubomír
  • Nováček, Jiří
  • Sklenář, Vladimír
  • Žídek, Lukáš
http://linked.open...ain/vavai/riv/wos
  • 000323661800001
issn
  • 0925-2738
number of pages
http://bibframe.org/vocab/doi
  • 10.1007/s10858-013-9761-7
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  • 14740
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