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

ABSTRACT: 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.

SUBMITTER: Zinke M

PROVIDER: S-EPMC6220863 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature

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

Zinke Maximilian M Fricke Pascal P Lange Sascha S Zinn-Justin Sophie S Lange Adam A

Chemphyschem : a European journal of chemical physics and physical chemistry 20180627 19

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. ...[more]

PMID: 29917302

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