EVANGELIDIS, Thomas, S. NERLI, Jiří NOVÁČEK, A.E. BRERETON, P.A. KARPLUS, R.R. DOTAS, V. VENDITTI, N.G. SGOURAKIS a Konstantinos TRIPSIANES. Automated NMR resonance assignments and structure determination using a minimal set of 4D spectra. Nature Communications. London: Nature Publishing Group, 2018, roč. 9, JAN, s. 384-396. ISSN 2041-1723. Dostupné z: https://dx.doi.org/10.1038/s41467-017-02592-z. |
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@article{1435119, author = {Evangelidis, Thomas and Nerli, S. and Nováček, Jiří and Brereton, A.E. and Karplus, P.A. and Dotas, R.R. and Venditti, V. and Sgourakis, N.G. and Tripsianes, Konstantinos}, article_location = {London}, article_number = {JAN}, doi = {http://dx.doi.org/10.1038/s41467-017-02592-z}, keywords = {PROTEIN-STRUCTURE DETERMINATION; CHEMICAL-SHIFTS; DIPOLAR COUPLINGS; NOESY ASSIGNMENT; LARGER PROTEINS; SPECTROSCOPY; ROSETTA; ROBUST; ALGORITHM; HOMOLOGY}, language = {eng}, issn = {2041-1723}, journal = {Nature Communications}, title = {Automated NMR resonance assignments and structure determination using a minimal set of 4D spectra}, url = {https://www.nature.com/articles/s41467-017-02592-z.pdf}, volume = {9}, year = {2018} }
TY - JOUR ID - 1435119 AU - Evangelidis, Thomas - Nerli, S. - Nováček, Jiří - Brereton, A.E. - Karplus, P.A. - Dotas, R.R. - Venditti, V. - Sgourakis, N.G. - Tripsianes, Konstantinos PY - 2018 TI - Automated NMR resonance assignments and structure determination using a minimal set of 4D spectra JF - Nature Communications VL - 9 IS - JAN SP - 384 EP - 384 PB - Nature Publishing Group SN - 20411723 KW - PROTEIN-STRUCTURE DETERMINATION KW - CHEMICAL-SHIFTS KW - DIPOLAR COUPLINGS KW - NOESY ASSIGNMENT KW - LARGER PROTEINS KW - SPECTROSCOPY KW - ROSETTA KW - ROBUST KW - ALGORITHM KW - HOMOLOGY UR - https://www.nature.com/articles/s41467-017-02592-z.pdf N2 - Automated methods for NMR structure determination of proteins are continuously becoming more robust. However, current methods addressing larger, more complex targets rely on analyzing 6-10 complementary spectra, suggesting the need for alternative approaches. Here, we describe 4D-CHAINS/autoNOE-Rosetta, a complete pipeline for NOE-driven structure determination of medium-to larger-sized proteins. The 4D-CHAINS algorithm analyzes two 4D spectra recorded using a single, fully protonated protein sample in an iterative ansatz where common NOEs between different spin systems supplement conventional through-bond connectivities to establish assignments of sidechain and backbone resonances at high levels of completeness and with a minimum error rate. The 4D-CHAINS assignments are then used to guide automated assignment of long-range NOEs and structure refinement in autoNOE-Rosetta. Our results on four targets ranging in size from 15.5 to 27.3 kDa illustrate that the structures of proteins can be determined accurately and in an unsupervised manner in a matter of days. ER -
EVANGELIDIS, Thomas, S. NERLI, Jiří NOVÁČEK, A.E. BRERETON, P.A. KARPLUS, R.R. DOTAS, V. VENDITTI, N.G. SGOURAKIS a Konstantinos TRIPSIANES. Automated NMR resonance assignments and structure determination using a minimal set of 4D spectra. \textit{Nature Communications}. London: Nature Publishing Group, 2018, roč.~9, JAN, s.~384-396. ISSN~2041-1723. Dostupné z: https://dx.doi.org/10.1038/s41467-017-02592-z.
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