Protein-Protein Interfaces Probed by Methyl Labeling and Proton-Detected Solid-State NMR Spectroscopy

Maximilian Zinke (1) , Pascal Fricke , Sascha Lange , Sophie Zinn-Justin (2, 3, 4) , Adam Lange

1 FMP - Leibniz Forschungsinstitut für Molekulare Pharmakolgie = Leibniz Institute for Molecular Pharmacology [Berlin, Allemagne]
2 INTGEN - Enveloppe Nucléaire, Télomères et Réparation de l’ADN
3 I2BC - Institut de Biologie Intégrative de la Cellule
4 B3S - Département Biochimie, Biophysique et Biologie Structurale

Proton detection and fast magic-angle spinning have advanced biological solid-state NMR, allowing for the backbone assignment of complex protein assemblies with high sensitivity and resolution. However, so far no method has been proposed to detect intermolecular interfaces in these assemblies by proton detection. Herein, we introduce a concept based on methyl labeling that allows for the assignment of these moieties and for the study of protein-protein interfaces at atomic resolution.

Mots clés: proteins; dynamics; SPP1; gp17.1; protein structures; angle-spinning nmr; backbone assignment; c-13; fibrils; h-1-h-1 distance restraints; interfaces; isoleucine; methyl labeling; methyl-labeling; multidimensional nmr; resonance assignment; rotating solids; Solid-State NMR

Domaines: Sciences du Vivant [q-bio]

Maximilian Zinke, Pascal Fricke, Sascha Lange, Sophie Zinn-Justin, Adam Lange. Protein-Protein Interfaces Probed by Methyl Labeling and Proton-Detected Solid-State NMR Spectroscopy. ChemPhysChem, 2018, 19 (19), pp.2457--2460. ⟨10.1002/cphc.201800542⟩. ⟨hal-02185072⟩