Journal of Biomolecular NMR, volume 63, issue 1, pages 85-95
MERA: a webserver for evaluating backbone torsion angle distributions in dynamic and disordered proteins from NMR data
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Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, USA
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Max Planck Institute of Biophysics, Frankfurt am Main, Germany
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Publication type: Journal Article
Publication date: 2015-07-29
Journal:
Journal of Biomolecular NMR
Quartile SCImago
Q1
Quartile WOS
Q2
Impact factor: 2.7
ISSN: 09252738, 15735001
PubMed ID:
26219516
Biochemistry
Spectroscopy
Abstract
MERA (Maximum Entropy Ramachandran map Analysis from NMR data) is a new webserver that generates residue-by-residue Ramachandran map distributions for disordered proteins or disordered regions in proteins on the basis of experimental NMR parameters. As input data, the program currently utilizes up to 12 different parameters. These include three different types of short-range NOEs, three types of backbone chemical shifts (15N, 13Cα, and 13C′), six types of J couplings (3JHNHα, 3JC′C′, 3JC′Hα, 1JHαCα, 2JCαN and 1JCαN), as well as the 15N-relaxation derived J(0) spectral density. The Ramachandran map distributions are reported in terms of populations of their 15° × 15° voxels, and an adjustable maximum entropy weight factor is available to ensure that the obtained distributions will not deviate more from a newly derived coil library distribution than required to account for the experimental data. MERA output includes the agreement between each input parameter and its distribution-derived value. As an application, we demonstrate performance of the program for several residues in the intrinsically disordered protein α-synuclein, as well as for several static and dynamic residues in the folded protein GB3.
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- We do not take into account publications that without a DOI.
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- Statistics recalculated weekly.
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Mantsyzov A. B. et al. MERA: a webserver for evaluating backbone torsion angle distributions in dynamic and disordered proteins from NMR data // Journal of Biomolecular NMR. 2015. Vol. 63. No. 1. pp. 85-95.
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Mantsyzov A. B., Shen Y., Lee J., Hummer G., Bax A. MERA: a webserver for evaluating backbone torsion angle distributions in dynamic and disordered proteins from NMR data // Journal of Biomolecular NMR. 2015. Vol. 63. No. 1. pp. 85-95.
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TY - JOUR
DO - 10.1007/S10858-015-9971-2
UR - https://doi.org/10.1007%2FS10858-015-9971-2
TI - MERA: a webserver for evaluating backbone torsion angle distributions in dynamic and disordered proteins from NMR data
T2 - Journal of Biomolecular NMR
AU - Lee, Jung-Ho
AU - Hummer, Gerhard
AU - Bax, Ad
AU - Mantsyzov, Alexey B
AU - Shen, Yang
PY - 2015
DA - 2015/07/29 00:00:00
PB - Springer Nature
SP - 85-95
IS - 1
VL - 63
PMID - 26219516
SN - 0925-2738
SN - 1573-5001
ER -
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@article{2015_Mantsyzov,
author = {Jung-Ho Lee and Gerhard Hummer and Ad Bax and Alexey B Mantsyzov and Yang Shen},
title = {MERA: a webserver for evaluating backbone torsion angle distributions in dynamic and disordered proteins from NMR data},
journal = {Journal of Biomolecular NMR},
year = {2015},
volume = {63},
publisher = {Springer Nature},
month = {jul},
url = {https://doi.org/10.1007%2FS10858-015-9971-2},
number = {1},
pages = {85--95},
doi = {10.1007/S10858-015-9971-2}
}
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MLA
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Mantsyzov, Alexey B., et al. “MERA: a webserver for evaluating backbone torsion angle distributions in dynamic and disordered proteins from NMR data.” Journal of Biomolecular NMR, vol. 63, no. 1, Jul. 2015, pp. 85-95. https://doi.org/10.1007%2FS10858-015-9971-2.
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