| EVANGELIDIS, Thomas, S. NERLI, Jiří NOVÁČEK, A.E. BRERETON, P.A. KARPLUS, R.R. DOTAS, V. VENDITTI, N.G. SGOURAKIS and Konstantinos TRIPSIANES. Automated NMR resonance assignments and structure determination using a minimal set of 4D spectra. Nature Communications. London: Nature Publishing Group, 2018, vol. 9, JAN, p. 384-396. ISSN 2041-1723. Available from: 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 and Konstantinos TRIPSIANES. Automated NMR resonance assignments and structure determination using a minimal set of 4D spectra. \textit{Nature Communications}. London: Nature Publishing Group, 2018, vol.~9, JAN, p.~384-396. ISSN~2041-1723. Available from: https://dx.doi.org/10.1038/s41467-017-02592-z.
|
