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@article{1123258, author = {Nováček, Jiří and Janda, Lubomír and Dopitová, Radka and Žídek, Lukáš and Sklenář, Vladimír}, article_location = {Dordrecht}, article_number = {4}, doi = {http://dx.doi.org/10.1007/s10858-013-9761-7}, keywords = {Nuclear magnetic resonance; Intrinsically disordered proteins; Microtubule-associated protein; Transient secondary structure; C-13 detection}, language = {eng}, issn = {0925-2738}, journal = {Journal of Biomolecular NMR}, 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}, url = {http://www.ncbi.nlm.nih.gov/pubmed/23877929}, volume = {56}, year = {2013} }
TY - JOUR ID - 1123258 AU - Nováček, Jiří - Janda, Lubomír - Dopitová, Radka - Žídek, Lukáš - Sklenář, Vladimír PY - 2013 TI - 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 JF - Journal of Biomolecular NMR VL - 56 IS - 4 SP - 291-301 EP - 291-301 PB - Springer SN - 09252738 KW - Nuclear magnetic resonance KW - Intrinsically disordered proteins KW - Microtubule-associated protein KW - Transient secondary structure KW - C-13 detection UR - http://www.ncbi.nlm.nih.gov/pubmed/23877929 L2 - http://www.ncbi.nlm.nih.gov/pubmed/23877929 N2 - 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. The obtained data provides the first atomic resolution insight into the conformational state of MAP2c and constitutes a model for further functional studies of MAPs. ER -
NOVÁČEK, Jiří, Lubomír JANDA, Radka DOPITOVÁ, Lukáš ŽÍDEK a Vladimír SKLENÁŘ. 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. \textit{Journal of Biomolecular NMR}. Dordrecht: Springer, 2013, roč.~56, č.~4, s.~291-301. ISSN~0925-2738. Dostupné z: https://dx.doi.org/10.1007/s10858-013-9761-7.
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