Abstract
Two experiments are presented that yield amino acid type identification of individual residues in a protein by editing the 1H–15N correlations into four different 2D subspectra, each corresponding to a different amino acid type class, and that can be applied to deuterated proteins. One experiment provides information on the amino acid type of the residue preceding the detected amide 1H–15N correlation, while the other gives information on the type of its own residue. Versions for protonated proteins are also presented, and in this case it is possible to classify the residues into six different classes. Both sequential and intraresidue experiments provide highly complementary information, greatly facilitating the assignment of protein resonances. The experiments will also assist in transferring the assignment of a protein to the spectra obtained under different experimental conditions (e.g. temperature, pH, presence of ligands, cofactors, etc.).
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This work was supported by projects CTQ2008-00080 and CTQ2011-22514 from the Spanish Ministerio de Ciencia e Innovación.
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Pantoja-Uceda, D., Santoro, J. New amino acid residue type identification experiments valid for protonated and deuterated proteins. J Biomol NMR 54, 145–153 (2012). https://doi.org/10.1007/s10858-012-9665-y
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DOI: https://doi.org/10.1007/s10858-012-9665-y