Magic angle spinning (MAS) solid-state NMR (ssNMR) is an established tool that can be applied to non-soluble or non-crystalline biomolecules of any size or complexity. The ssNMR method advances rapidly due to technical improvements and the development of advanced isotope labeling schemes. While ssNMR has shown significant progress in structural studies of proteins, the number of RNA studies remains limited due to ssNMR methodology that is still underdeveloped. Resonance assignment is the most...
[NMR paper] Identification of RNA base pairs and complete assignment of nucleobase resonances by 1H-detected solid-state NMR spectroscopy at 100 kHz MAS
Identification of RNA base pairs and complete assignment of nucleobase resonances by 1H-detected solid-state NMR spectroscopy at 100 kHz MAS
Knowledge of RNA structure, either in isolation or in complex, is fundamental to understand the mechanism of cellular processes. Solid-state NMR (ssNMR) is applicable to high molecular-weight complexes and does not require crystallization; thus, it is well-suited to study RNA as part of large multicomponent assemblies. Recently, we solved the first structures of both RNA and an RNA-protein complex by ssNMR using conventional 13 C- and 15 N-detection....
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08-12-2021 08:56 AM
[NMR paper] Resonance assignment of the outer membrane protein AlkL in lipid bilayers by proton-detected solid-state NMR.
Resonance assignment of the outer membrane protein AlkL in lipid bilayers by proton-detected solid-state NMR.
Related Articles Resonance assignment of the outer membrane protein AlkL in lipid bilayers by proton-detected solid-state NMR.
Biomol NMR Assign. 2020 Jun 30;:
Authors: Schubeis T, Schwarzer TS, Le Marchand T, Stanek J, Movellan KT, Castiglione K, Pintacuda G, Andreas LB
Abstract
Most commonly small outer membrane proteins, possessing between 8 and 12 ?-strands, are not involved in transport but fulfill diverse functions...
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07-02-2020 11:18 AM
[NMR paper] Towards automatic protein backbone assignment using proton-detected 4D solid-state NMR data.
Towards automatic protein backbone assignment using proton-detected 4D solid-state NMR data.
Related Articles Towards automatic protein backbone assignment using proton-detected 4D solid-state NMR data.
J Biomol NMR. 2014 Sep 6;
Authors: Xiang S, Chevelkov V, Becker S, Lange A
Abstract
We introduce an efficient approach for sequential protein backbone assignment based on two complementary proton-detected 4D solid-state NMR experiments that correlate /Ni with CAi/COi or CAi-1/COi-1. The resulting 4D spectra exhibit excellent...
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09-07-2014 12:36 PM
Towards automatic protein backbone assignment using proton-detected 4D solid-state NMR data
Towards automatic protein backbone assignment using proton-detected 4D solid-state NMR data
Abstract
We introduce an efficient approach for sequential protein backbone assignment based on two complementary proton-detected 4D solid-state NMR experiments that correlate \( {\text{H}}_{{\text{i}}}^{{\text{N}}} \) /Ni with CAi/COi or CAiâ??1/COiâ??1. The resulting 4D spectra exhibit excellent sensitivity and resolution and are amenable to (semi-)automatic assignment...
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09-06-2014 07:41 AM
[NMR paper] Out-and-back (13)C- (13)C scalar transfers in protein resonance assignment by proton-detected solid-state NMR under ultra-fast MAS.
Out-and-back (13)C- (13)C scalar transfers in protein resonance assignment by proton-detected solid-state NMR under ultra-fast MAS.
Related Articles Out-and-back (13)C- (13)C scalar transfers in protein resonance assignment by proton-detected solid-state NMR under ultra-fast MAS.
J Biomol NMR. 2013 Jun 29;
Authors: Barbet-Massin E, Pell AJ, Jaudzems K, Franks WT, Retel JS, Kotelovica S, Akopjana I, Tars K, Emsley L, Oschkinat H, Lesage A, Pintacuda G
Abstract
We present here (1)H-detected triple-resonance H/N/C experiments that...
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07-03-2013 01:46 PM
[NMR paper] (13) C-Detected Through-Bond Correlation Experiments for Protein Resonance Assignment by Ultra-Fast MAS Solid-State NMR.
(13) C-Detected Through-Bond Correlation Experiments for Protein Resonance Assignment by Ultra-Fast MAS Solid-State NMR.
Related Articles (13) C-Detected Through-Bond Correlation Experiments for Protein Resonance Assignment by Ultra-Fast MAS Solid-State NMR.
Chemphyschem. 2013 Apr 15;
Authors: Barbet-Massin E, Pell AJ, Knight MJ, Webber AL, Felli IC, Pierattelli R, Emsley L, Lesage A, Pintacuda G
Abstract
We present two sequences which combine ((1) H,(15) N) and ((15) N,(13) C) selective cross-polarization steps with an efficient variant...
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04-17-2013 08:15 PM
Assignment strategies for aliphatic protons in the solid-state in randomly protonated proteins
Assignment strategies for aliphatic protons in the solid-state in randomly protonated proteins
Abstract Biological solid-state nuclear magnetic resonance spectroscopy developed rapidly in the past two decades and emerged as an important tool for structural biology. Resonance assignment is an essential prerequisite for structure determination and the characterization of motional properties of a molecule. Experiments, which rely on carbon or nitrogen detection, suffer, however, from low sensitivity. Recently, we introduced the RAP (Reduced Adjoining Protonation) labeling scheme, which...