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Site-Specific Detection of Arginine Methylation in Highly Repetitive Protein Motifs of Low Sequence Complexity by NMR.
Altincekic, Nadide; Löhr, Frank; Meier-Credo, Jakob; Langer, Julian D; Hengesbach, Martin; Richter, Christian; Schwalbe, Harald.
Afiliación
  • Altincekic N; Institute for Organic Chemistry and Chemical Biology, Goethe University Frankfurt am Main, Frankfurt 60438, Germany.
  • Löhr F; Center of Biomolecular Magnetic Resonance (BMRZ), Goethe University Frankfurt am Main, Frankfurt 60438, Germany.
  • Meier-Credo J; Center of Biomolecular Magnetic Resonance (BMRZ), Goethe University Frankfurt am Main, Frankfurt 60438, Germany.
  • Langer JD; Institute of Biophysical Chemistry, Goethe University Frankfurt am Main, Frankfurt 60438, Germany.
  • Hengesbach M; Max Planck Institute of Biophysics, Frankfurt am Main, 60438, Germany.
  • Richter C; Max Planck Institute of Biophysics, Frankfurt am Main, 60438, Germany.
  • Schwalbe H; Institute for Organic Chemistry and Chemical Biology, Goethe University Frankfurt am Main, Frankfurt 60438, Germany.
J Am Chem Soc ; 142(16): 7647-7654, 2020 04 22.
Article en En | MEDLINE | ID: mdl-32233470
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.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Arginina / Espectroscopía de Resonancia Magnética / Proteínas Tipo de estudio: Diagnostic_studies Límite: Humans Idioma: En Revista: J Am Chem Soc Año: 2020 Tipo del documento: Article País de afiliación: Alemania

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Arginina / Espectroscopía de Resonancia Magnética / Proteínas Tipo de estudio: Diagnostic_studies Límite: Humans Idioma: En Revista: J Am Chem Soc Año: 2020 Tipo del documento: Article País de afiliación: Alemania