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Journal Article

Site-Specific Detection of Arginine Methylation in Highly Repetitive Protein Motifs of Low Sequence Complexity by NMR

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Meier-Credo,  Jakob       
Proteomics and Mass Spectrometry, Max Planck Institute of Biophysics, Max Planck Society;

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Langer,  Julian David       
Proteomics and Mass Spectrometry, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Altincekic, N., Löhr, F., Meier-Credo, J., Langer, J. D., Hengesbach, M., Richter, C., et al. (2020). Site-Specific Detection of Arginine Methylation in Highly Repetitive Protein Motifs of Low Sequence Complexity by NMR. Journal of the American Chemical Society, 142(16), 7647-7654. doi:10.1021/jacs.0c02308.


Cite as: https://hdl.handle.net/21.11116/0000-0006-7B35-5
Abstract
Post-translational modifications of proteins are widespread in eukaryotes. To elucidate the functional role of these modifications, detection methods need to be developed that provide information at atomic resolution. Here, we report on the development of a novel Arg-specific NMR experiment that detects the methylation status and symmetry of each arginine side chain even in highly repetitive RGG amino acid sequence motifs found in numerous proteins within intrinsically disordered regions. The experiment relies on the excellent resolution of the backbone H,N correlation spectra even in these low complexity sequences. It requires 13C, 15N labeled samples.