Ultrafast high-resolution magic-angle-spinning NMR spectroscopy

André, Marion; Piotto, Martial; Caldarelli, Stéfano; Dumez, Jean‐Nicolas

doi:10.1039/c5an00653h

Cited by 14 publications

(13 citation statements)

References 27 publications

(13 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Membrane proteins that can only be obtained in relatively small quantities (hundreds of micrograms or less) will benefit from technical developments that improve resolution and sensitivity. Recent such developments include microcoil MAS and microsamples (Takeda, 2012), fast MAS at 100 kHz and above (Agarwal et al, 2014;André et al, 2015;Böckmann et al, 2015), MAS with the sample at cryogenic temperatures (Barnes et al, 2009;Concistrè et al, 2013;Thurber & Tycko, 2008;Tycko, 2013), DNP-enhanced MAS (Akbey et al, 2013;Koers et al, 2014;Maciejko et al, 2015;Smith et al, 2015;Su et al, 2015) and higher field (1 GHz plus) magnets (Hashi et al, 2015). Deuteration of the protein and sample allows acquisition of high-resolution solid-state NMR proton spectra that are useful for membrane protein structure determination (Reif, 2012), it also improves T 2 relaxation times and resolution that facilitate sequential backbone assignments using 13 C-detected experiments (Tang et al, 2010).…”

Section: Conclusion and Future Perspectivesmentioning

confidence: 99%

Solid-state NMR structures of integral membrane proteins

Patching¹

2015

Molecular Membrane Biology

View full text Add to dashboard Cite

Solid-state NMR is unique for its ability to obtain three-dimensional structures and to measure atomic-resolution structural and dynamic information for membrane proteins in native lipid bilayers. An increasing number and complexity of integral membrane protein structures have been determined by solid-state NMR using two main methods. Oriented sample solid-state NMR uses macroscopically aligned lipid bilayers to obtain orientational restraints that define secondary structure and global fold of embedded peptides and proteins and their orientation and topology in lipid bilayers. Magic angle spinning (MAS) solid-state NMR uses unoriented rapidly spinning samples to obtain distance and torsion angle restraints that define tertiary structure and helix packing arrangements. Details of all current protein structures are described, highlighting developments in experimental strategy and other technological advancements. Some structures originate from combining solid- and solution-state NMR information and some have used solid-state NMR to refine X-ray crystal structures. Solid-state NMR has also validated the structures of proteins determined in different membrane mimetics by solution-state NMR and X-ray crystallography and is therefore complementary to other structural biology techniques. By continuing efforts in identifying membrane protein targets and developing expression, isotope labelling and sample preparation strategies, probe technology, NMR experiments, calculation and modelling methods and combination with other techniques, it should be feasible to determine the structures of many more membrane proteins of biological and biomedical importance using solid-state NMR. This will provide three-dimensional structures and atomic-resolution structural information for characterising ligand and drug interactions, dynamics and molecular mechanisms of membrane proteins under physiological lipid bilayer conditions.

show abstract

Section: Conclusion and Future Perspectivesmentioning

confidence: 99%

Solid-state NMR structures of integral membrane proteins

Patching¹

2015

Molecular Membrane Biology

View full text Add to dashboard Cite

show abstract

“…The acquisition of ultrafast 2D spectra of semisolid samples, with a HR-MAS setup, was also recently demonstrated [57]. This approach is perfectly compatible with high-throughput studies or the analysis of fragile samples.…”

Section: Ultrafast Dq Spectroscopymentioning

confidence: 96%

Multiple-Quantum NMR Studies on Molecular Mixtures

Caldarelli¹,

Yemloul²

2016

Annual Reports on NMR Spectroscopy

Self Cite

View full text Add to dashboard Cite

“…Based on the concept of imparting a spatiotemporal encoding of the spin interactions to be measured using gradient sliceselective excitation. [33,[39][40][41][42][43][44][45][46][47][48][49][50][51][52] Hadamard NMR spectroscopy Based on simultaneous multisite selective excitation, employing encoding of phases of signals using Hadamard matrix [53][54][55] Fast-pulsing methods Using very short interscan or relaxation delays period by optimizing the flip angle of the excitation pulse [56][57][58][59] multiple receiver coils with improved sensitivity and resolution. [61,62] The two main modes of utilizing multiple receivers in NMR experiments are either parallel or sequential acquisition.…”

Section: Acquisition With Multiple Receiversmentioning

confidence: 99%

“…In addition to these two categories, another type of sampling approach involves multiple receivers [29,30] and ultrafast single-scan NMR techniques. [33,[39][40][41][42][43][44][45][46][47][48][49][50][51][52] This is summarized in Table 1. In this review, our discussions will be based more on fast NMR methods that have been developed in our group for the analysis of various metabolomics samples.…”

Section: Nmr Data Acquisition With High Sensitivity and Resolutionmentioning

confidence: 99%

Rapid nuclear magnetic resonance data acquisition with improved resolution and sensitivity for high‐throughput metabolomic analysis

Joseph

Sukumaran

Chandra

et al. 2020

Magnetic Reson in Chemistry

View full text Add to dashboard Cite

Nuclear magnetic resonance (NMR)-based metabolomics has witnessed rapid advancements in recent years with the continuous development of new methods to enhance the sensitivity, resolution, and speed of data acquisition. Some of the approaches were earlier used for peptide and protein resonance assignments and have now been adapted to metabolomics. At the same time, new NMR methods involving novel data acquisition techniques, suited particularly for high-throughput analysis in metabolomics, have been developed. In this review, we focus on the different sampling strategies or data acquisition methods that have been developed in our laboratory and other groups to acquire NMR spectra rapidly with high sensitivity and resolution for metabolomics. In particular, we focus on the use of multiple receivers, phase modulation NMR spectroscopy, and fast-pulsing methods for identification and assignments of metabolites.

show abstract

Ultrafast high-resolution magic-angle-spinning NMR spectroscopy

Cited by 14 publications

References 27 publications

Solid-state NMR structures of integral membrane proteins

Solid-state NMR structures of integral membrane proteins

Multiple-Quantum NMR Studies on Molecular Mixtures

Rapid nuclear magnetic resonance data acquisition with improved resolution and sensitivity for high‐throughput metabolomic analysis

Contact Info

Product

Resources

About