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.
Keywords: interfaces; methyl labeling; protein structures; proteins; solid-state NMR.
© 2018 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.