Backbone assignments and conformational dynamics in the S. typhimurium tryptophan synthase α-subunit from solution-state NMR
Author:
Funder
National Science Foundation
National Institutes of Health
Publisher
Springer Science and Business Media LLC
Subject
Spectroscopy,Biochemistry
Link
https://link.springer.com/content/pdf/10.1007/s10858-020-00320-2.pdf
Reference75 articles.
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2. Axe JM, Boehr DD (2013) Long-range interactions in the alpha subunit of tryptophan synthase help to coordinate ligand binding, catalysis, and substrate channeling. J Mol Biol 425:1527–1545. https://doi.org/10.1016/j.jmb.2013.01.030
3. Axe JM, Yezdimer EM, O’Rourke KF, Kerstetter NE, You W, Chang CA, Boehr DD (2014) Amino acid networks in a (β/α)8 barrel enzyme change during catalytic turnover. J Am Chem Soc 136:6818–6821. https://doi.org/10.1021/ja501602t
4. Bahrami A, Assadi AH, Markley JL, Eghbalnia HR (2009) Probabilistic interaction network of evidence algorithm and its application to complete labeling of peak lists from protein NMR spectroscopy. PLoS Comput Biol 5:1–15. https://doi.org/10.1371/journal.pcbi.1000307
5. Barends TRM, Domratcheva T, Kulik V, Blumenstein L, Niks D, Dunn MF, Schlichting I (2008a) Structure and mechanistic implications of a tryptophan synthase quinonoid intermediate. ChemBioChem 9:1024–1028. https://doi.org/10.1002/cbic.200700703
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