1. Protein−Protein Interfaces Probed by Methyl Labeling and Proton-Detected Solid-State NMR Spectroscopy
- Author
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Pascal Fricke, Sophie Zinn-Justin, Adam Lange, Sascha Lange, Maximilian Zinke, Leibniz Forschungsinstitut für Molekulare Pharmakolgie = Leibniz Institute for Molecular Pharmacology [Berlin, Allemagne] (FMP), Leibniz Association, Enveloppe Nucléaire, Télomères et Réparation de l’ADN (INTGEN), Département Biochimie, Biophysique et Biologie Structurale (B3S), Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)
- Subjects
multidimensional nmr ,fibrils ,gp17.1 ,0301 basic medicine ,Materials science ,Proton ,[SDV]Life Sciences [q-bio] ,methyl-labeling ,isoleucine ,010402 general chemistry ,01 natural sciences ,interfaces ,03 medical and health sciences ,Protein structure ,rotating solids ,Atomic resolution ,Amino Acid Sequence ,Physical and Theoretical Chemistry ,Spectroscopy ,Nuclear Magnetic Resonance, Biomolecular ,resonance assignment ,Glycoproteins ,Quantitative Biology::Biomolecules ,Communication ,Quantitative Biology::Molecular Networks ,Protein protein ,Resolution (electron density) ,Intermolecular force ,angle-spinning nmr ,methyl labeling ,c-13 ,dynamics ,Communications ,proteins ,Atomic and Molecular Physics, and Optics ,Protein Structure, Tertiary ,backbone assignment ,3. Good health ,0104 chemical sciences ,Crystallography ,030104 developmental biology ,Solid-state nuclear magnetic resonance ,protein structures ,h-1-h-1 distance restraints ,Protons ,SPP1 ,Solid-State NMR - Abstract
International audience; 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.
- Published
- 2018
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