Fast magic-angle sample spinning solid-state NMR at 60–100 kHz for natural abundance samples

Nishiyama, Yusuke

doi:10.1016/j.ssnmr.2016.06.002

Cited by 131 publications

(245 citation statements)

References 138 publications

Supporting

Mentioning

240

Contrasting

Order By: Relevance

“…In fact, the maximum achievable spinning frequency ( ν max ) is inversely proportional to the rotor diameter ( d ) according to a simple relationship ν max ≈ 80 kHz·mm/ d , considering the influences of bearing load, strength of rotor materials, turbine torques, and other factors as well. 6 In further combination with appropriate deuteration and high magnetic fields, it has been possible to achieve solution-like proton NMR spectra even in proteins, which has attracted much attention in recent years. 7–11 In fact, the discovery and demonstration of new phenomena under ultrafast MAS has also greatly simplified the design of pulse sequences and experimental setup.…”

Section: Introductionmentioning

confidence: 99%

Proton-Based Ultrafast Magic Angle Spinning Solid-State NMR Spectroscopy

2017

View full text Add to dashboard Cite

CONSPECTUS Protons are vastly abundant in a wide range of exciting macromolecules and thus can be a powerful probe to investigate the structure and dynamics at atomic resolution using solid-state NMR (ssNMR) spectroscopy. Unfortunately, the high signal sensitivity, afforded by the high natural-abundance and high gyromagnetic ratio of protons, is greatly compromised by severe line broadening due to the very strong 1H–1H dipolar couplings. As a result, protons are rarely used, in spite of the desperate need for enhancing the sensitivity of ssNMR to study a variety of systems that are not amenable for high resolution investigation using other techniques including X-ray crystallography, cryo-electron microscopy, and solution NMR spectroscopy. Thanks to the remarkable improvement in proton spectral resolution afforded by the significant advances in magic-angle-spinning (MAS) probe technology, 1H ssNMR spectroscopy has recently attracted considerable attention in the structural and dynamics studies of various molecular systems. However, it still remains a challenge to obtain narrow 1H spectral lines, especially from proteins, without resorting to deuteration. In this Account, we review recent proton-based ssNMR strategies that have been developed in our laboratory to further improve proton spectral resolution without resorting to chemical deuteration for the purposes of gaining atomistic-level insights into molecular structures of various crystalline solid systems, using small molecules and peptides as illustrative examples. The proton spectral resolution enhancement afforded by the ultrafast MAS frequencies up to 120 kHz is initially discussed, followed by a description of an ensemble of multidimensional NMR pulse sequences, all based on proton detection, that have been developed to obtain in-depth information from dipolar couplings and chemical shift anisotropy (CSA). Simple single channel multidimensional proton NMR experiments could be performed to probe the proximity of protons for structure determination using 1H–1H dipolar couplings and to evaluate the changes in chemical environments as well as the relative orientation to the external magnetic field using proton CSA. Due to the boost in signal sensitivity enabled by proton detection under ultrafast MAS, by virtue of high proton natural abundance and gyromagnetic ratio, proton-detected multidimensional experiments involving low-γ nuclei can now be accomplished within a reasonable time, while the higher dimension also offers additional resolution enhancement. In addition, the application of proton-based ssNMR spectroscopy under ultrafast MAS in various challenging and crystalline systems is also presented. Finally, we briefly discuss the limitations and challenges pertaining to proton-based ssNMR spectroscopy under ultrafast MAS conditions, such as the presence of high-order dipolar couplings, friction-induced sample heating, and limited sample volume. Although there are still a number of challenges that must be circumvented by further developments in radio freq...

show abstract

Section: Introductionmentioning

confidence: 99%

Proton-Based Ultrafast Magic Angle Spinning Solid-State NMR Spectroscopy

2017

View full text Add to dashboard Cite

show abstract

“…In spite of these challenges the numerous applications enabled by CRAMPS are a testament to desirability and wide scope of applications of 1 H spectroscopy. The promise to achieve similar or better resolution as the one afforded by CRAMPS methods but without the associated challenges renders 1 H spectroscopy enabled by fast spinning highly desirable [37]. To guide such experiments and to understand their intrinsic limitations, in this contribution we estimate the extent to which the powder lines can be narrowed by MAS.…”

Section: Introductionmentioning

confidence: 99%

1H line width dependence on MAS speed in solid state NMR – Comparison of experiment and simulation

Sternberg

Witter

Kuprov

et al. 2018

Journal of Magnetic Resonance

View full text Add to dashboard Cite

b s t r a c tRecent developments in magic angle spinning (MAS) technology permit spinning frequencies of !100 kHz. We examine the effect of such fast MAS rates upon nuclear magnetic resonance proton line widths in the multi-spin system of b-Asp-Ala crystal. We perform powder pattern simulations employing Fokker-Plank approach with periodic boundary conditions and 1 H-chemical shift tensors calculated using the bond polarization theory. The theoretical predictions mirror well the experimental results. Both approaches demonstrate that homogeneous broadening has a linear-quadratic dependency on the inverse of the MAS spinning frequency and that, at the faster end of the spinning frequencies, the residual spectral line broadening becomes dominated by chemical shift distributions and susceptibility effects even for crystalline systems.

show abstract

“…However, due to strong homonuclear dipolar interactions and limited chemical shift spread, it is not easy to obtain well‐resolved solid‐state 1 H NMR spectra. In recent years, this problem has been addressed and resolution increased significantly by the use of ultra‐high‐speed magic‐angle spinning employing spinning speeds up to 120 kHz (Agarwal et al, ; Nishiyama, ). The use of heteronuclear correlation experiments (Burum et al, ; Elena et al, ; Lesage, Sakellariou, et al, ), also helps in reducing spectral crowding in the proton dimension through well‐dispersed 13 C/ 15 N chemical shifts.…”

Section: Methodsmentioning

confidence: 99%

Conformational investigation of peptides using solid‐state NMR spectroscopy—A study of polymorphism of β‐turn peptides containing diprolines

et al. 2019

Self Cite

View full text Add to dashboard Cite

The construction of complex protein folds relies on the precise conversion of a linear polypeptide chain into a compact 3‐dimensional structure. In this context, study of isolated secondary structural modules containing short stretches of amino acids assumes significance. Additionally, peptides, both natural and synthetic, play a major role as potential drugs. With a view to understand the local conformations adopted by peptides in the solid state, we propose a multinuclear NMR approach utilizing spectra of nuclei in their natural isotopic abundance. Various solid‐state NMR experiments have been utilized for assignment of the spectra. Additionally, the gauge‐including projector augmented‐wave (GIPAW) calculations were used to confirm the assignments. Particularly, the utility of the double‐quantum–single‐quantum correlation experiments is highlighted for the purpose of assignment and for inferring the conformation across the peptide bond. The methodology is illustrated for the case of designed peptides containing diproline residues occurring at the β‐turns for identifying their cis‐trans conformational polymorphism. The proposed method promises to be of use in the study of conformations of small‐ to medium‐sized peptides such as antimicrobial peptides and in the study of polymorphism leading to applications in drug development protocols.

show abstract

Fast magic-angle sample spinning solid-state NMR at 60–100 kHz for natural abundance samples

Cited by 131 publications

References 138 publications

Proton-Based Ultrafast Magic Angle Spinning Solid-State NMR Spectroscopy

Proton-Based Ultrafast Magic Angle Spinning Solid-State NMR Spectroscopy

1H line width dependence on MAS speed in solid state NMR – Comparison of experiment and simulation

Conformational investigation of peptides using solid‐state NMR spectroscopy—A study of polymorphism of β‐turn peptides containing diprolines

Contact Info

Product

Resources

About