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Open AccessJournal ArticleDOI

Protein NMR Spectroscopy at 150 kHz Magic-Angle Spinning Continues To Improve Resolution and Mass Sensitivity

TLDR
It is concluded that even faster MAS is highly attractive and increases mass sensitivity at a moderate price in overall sensitivity.
Abstract
Spectral resolution is the key to unleashing the structural and dynamic information contained in NMR spectra. Fast magic-angle spinning (MAS) has recently revolutionized the spectroscopy of biomolecular solids. Herein, we report a further remarkable improvement in the resolution of the spectra of four fully protonated proteins and a small drug molecule by pushing the MAS rotation frequency higher (150 kHz) than the more routinely used 100 kHz. We observed a reduction in the average homogeneous linewidth by a factor of 1.5 and a decrease in the observed linewidth by a factor 1.25. We conclude that even faster MAS is highly attractive and increases mass sensitivity at a moderate price in overall sensitivity.

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Citations
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Structure of Fully Protonated Proteins by Proton-Detected Magic-Angle Spinning NMR

TL;DR: In this article, the authors used magic-angle spinning (MAS) to detect resolved 1H resonances in protonated proteins by increasing MAS rates to frequencies of 100 kHz and above.
Journal ArticleDOI

Solid-State NMR for Studying the Structure and Dynamics of Viral Assemblies

TL;DR: The way from first solid-state NMR investigations to the state-of-the-art approaches currently developing is traced, including applications focused on HIV, HBV, HCV and influenza, and an outlook to the possibilities opening in the coming years.
Journal ArticleDOI

Proton Detected Solid-State NMR of Membrane Proteins at 28 Tesla (1.2 GHz) and 100 kHz Magic-Angle Spinning.

TL;DR: The available magnetic field strength for high resolution NMR in persistent superconducting magnets has recently improved from 23.5 to 28 Tesla, increasing the proton resonance frequency from 1 to 1.2 GHz as mentioned in this paper.
Journal ArticleDOI

1H-Detected Biomolecular NMR under Fast Magic-Angle Spinning

TL;DR: The many examples where 1H-detected MAS NMR has contributed to the detailed characterization of a variety of crystalline and noncrystalline biomolecular targets involved in biological processes ranging from catalysis through drug binding, viral infectivity, amyloid fibril formation, to transport across lipid membranes are outlined.
References
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Journal ArticleDOI

Modelling one- and two-dimensional solid-state NMR spectra†

TL;DR: In this article, the authors present some examples of modeling one and two-dimensional solid-state NMR spectra of I = ½ spin and quadrupolar nuclei, using laboratory-developed software that is made available to the NMR community.
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Dynamic personalities of proteins.

TL;DR: The dream is to 'watch' proteins in action in real time at atomic resolution, which requires addition of a fourth dimension, time, to structural biology so that the positions in space and time of all atoms in a protein can be described in detail.
Journal ArticleDOI

Nuclear Magnetic Resonance Spectra from a Crystal rotated at High Speed

E. R. Andrew, +2 more
- 13 Dec 1958 - 
TL;DR: In this article, it was shown that when these weak side-spectra are included the second moment does indeed remain invariant even though the second moments of the central portion, which is all that is observed experimentally, becomes smaller.
Journal ArticleDOI

Amyloid fibrils of the HET-s(218–289) prion form a β-solenoid with a triangular hydrophobic core.

TL;DR: A structural model based on solid-state nuclear magnetic resonance restraints for amyloid fibrils from the prion-forming domain (residues 218 to 289) of the HET-s protein from the filamentous fungus Podospora anserina is presented.
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