Protein structure prediction assisted with sparse NMR data in CASP13

CASP13 has investigated the impact of sparse NMR data on the accuracy of protein structure prediction. NOESY and 15N‐1H residual dipolar coupling data, typical of that obtained for 15N,13C‐enriched, perdeuterated proteins up to about 40 kDa, were simulated for 11 CASP13 targets ranging in size from...

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Veröffentlicht in:	Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2019-12, Vol.87 (12), p.1315-1332
Hauptverfasser:	Sala, Davide, Huang, Yuanpeng Janet, Cole, Casey A., Snyder, David A., Liu, Gaohua, Ishida, Yojiro, Swapna, G.V.T., Brock, Kelly P., Sander, Chris, Fidelis, Krzysztof, Kryshtafovych, Andriy, Inouye, Masayori, Tejero, Roberto, Valafar, Homayoun, Rosato, Antonio, Montelione, Gaetano T.
Format:	Artikel
Sprache:	eng
Schlagworte:	Accuracy CASP Computer simulation contact prediction Dipole interactions Model accuracy Nitrogen isotopes NMR Nuclear magnetic resonance protein modeling Protein structure Proteins residual dipolar coupling simulated NMR spectra sparse NMR data Structural models structure prediction
Online-Zugang:	Volltext
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