Automatic 13C chemical shift reference correction for unassigned protein NMR spectra
Author:
Funder
National Science Foundation
National Institutes of Health
Publisher
Springer Science and Business Media LLC
Subject
Spectroscopy,Biochemistry
Link
http://link.springer.com/article/10.1007/s10858-018-0202-5/fulltext.html
Reference52 articles.
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2. Aramini JM, Mills JL, Xiao R, Acton TB, Wu MJ, Szyperski T, Montelione GT (2003a) Letter to the editor: resonance assignments for the hypothetical protein yggU from Escherichia coli. J Biomol NMR 27(3):285–286
3. Aramini JM, Huang YJ, Cort JR et al (2003b) Solution NMR structure of the 30S ribosomal protein S28E from Pyrococcus horikoshii. Protein Sci 12:2823–2830. https://doi.org/10.1110/ps.03359003
4. Barette J, Velyvis A, Religa TL et al (2011) Cross-validation of the structure of a transiently formed and low populated FF domain folding intermediate determined by relaxation dispersion NMR and CS-Rosetta. J Phys Chem B 116:6637–6644. https://doi.org/10.1021/jp209974f
5. Berman H, Henrick K, Nakamura H, Markley JL (2006) The worldwide Protein Data Bank (wwPDB): ensuring a single, uniform archive of PDB data. Nucleic Acids Res 35(suppl_1):D301–D303
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