Histidine residues play important structural and functional roles in proteins, such as serving as metal-binding ligands, mediating enzyme catalysis, and modulating proton channel activity. Many of these activities are modulated by the ionization state of the imidazole ring. Here we present a fast MAS NMR approach for the determination of protonation and tautomeric states of His at frequencies of 40-62 kHz. The experiments combine ¹H detection with selective magnetization inversion techniques and...
[NMR paper] Setting the magic angle for fast magic-angle spinning probes
Setting the magic angle for fast magic-angle spinning probes
Publication date: August 2018
Source: Journal of Magnetic Resonance, Volume 293
Author(s): Susanne Penzel, Albert A. Smith, Matthias Ernst, Beat H. Meier
Abstract
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[NMR paper] Setting the magic angle for fast magic-angle spinning probes
Setting the magic angle for fast magic-angle spinning probes
Publication date: Available online 15 June 2018
Source:Journal of Magnetic Resonance</br>
Author(s): Susanne Penzel, Albert A. Smith, Matthias Ernst, Beat H. Meier</br>
Fast magic-angle spinning, coupled with 1H detection is a powerful method to improve spectral resolution and signal to noise in solid-state NMR spectra. Commercial probes now provide spinning frequencies in excess of 100 kHz. Then, one has sufficient resolution in the 1H dimension to directly detect protons, which have a gyromagnetic...
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[NMR paper] Rapid measurement of long-range distances in proteins by multidimensional 13C-19F REDOR NMR under fast magic-angle spinning.
Rapid measurement of long-range distances in proteins by multidimensional 13C-19F REDOR NMR under fast magic-angle spinning.
Related Articles Rapid measurement of long-range distances in proteins by multidimensional 13C-19F REDOR NMR under fast magic-angle spinning.
J Biomol NMR. 2018 May 21;:
Authors: Shcherbakov AA, Hong M
Abstract
The ability to simultaneously measure many long-range distances is critical to efficient and accurate determination of protein structures by solid-state NMR (SSNMR). So far, the most common distance...
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Rapid measurement of long-range distances in proteins by multidimensional 13 Câ?? 19 F REDOR NMR under fast magic-angle spinning
Rapid measurement of long-range distances in proteins by multidimensional 13 Câ?? 19 F REDOR NMR under fast magic-angle spinning
Abstract
The ability to simultaneously measure many long-range distances is critical to efficient and accurate determination of protein structures by solid-state NMR (SSNMR). So far, the most common distance constraints for proteins are 13Câ??15N distances, which are usually measured using the rotational-echo double-resonance (REDOR) technique. However, these measurements are restricted to distances of up to ~â??5Â*Ã? due to...
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[NMR paper] Fast Magic-Angle-Spinning 19F Spin Exchange NMR for Determining Nanometer 19F-19F Distances in Proteins and Pharmaceutical Compounds.
Fast Magic-Angle-Spinning 19F Spin Exchange NMR for Determining Nanometer 19F-19F Distances in Proteins and Pharmaceutical Compounds.
Fast Magic-Angle-Spinning 19F Spin Exchange NMR for Determining Nanometer 19F-19F Distances in Proteins and Pharmaceutical Compounds.
J Phys Chem B. 2018 Feb 27;:
Authors: Roos M, Wang T, Shcherbakov AA, Hong M
Abstract
Internuclear distances measured using NMR provide crucial constraints of three-dimensional structures, but are often restricted to about 5 Å due to the weakness of nuclear-spin...
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02-28-2018 03:32 PM
[NMR paper] Rapid proton-detected NMR assignment for proteins with fast magic angle spinning.
Rapid proton-detected NMR assignment for proteins with fast magic angle spinning.
Rapid proton-detected NMR assignment for proteins with fast magic angle spinning.
J Am Chem Soc. 2014 Aug 7;
Authors: Barbet-Massin E, Pell AJ, Retel J, Andreas LB, Jaudzems K, Franks WT, Nieuwkoop AJ, Hiller M, Higman VA, Guerry P, Bertarello A, Knight MJ, Felletti M, Le Marchand T, Kotelovica S, Akopjana I, Tars K, Stoppini M, Bellotti V, Bolognesi M, Ricagno S, Chou JJ, Griffin RG, Oschkinat H, Lesage A, Emsley L, Herrmann T, Pintacuda G
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...
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Protonation, Tautomerization, and Rotameric Structure of Histidine: A Comprehensive Study by Magic-Angle-Spinning Solid-State NMR.
Protonation, Tautomerization, and Rotameric Structure of Histidine: A Comprehensive Study by Magic-Angle-Spinning Solid-State NMR.
Protonation, Tautomerization, and Rotameric Structure of Histidine: A Comprehensive Study by Magic-Angle-Spinning Solid-State NMR.
J Am Chem Soc. 2011 Jan 5;
Authors: Li S, Hong M
Histidine structure and chemistry lie at the heart of many enzyme active sites, ion channels, and metalloproteins. While solid-state NMR spectroscopy has been used to study histidine chemical shifts, the full pH dependence of the...
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Protonation, Tautomerization, and Rotameric Structure of Histidine: A Comprehensive Study by Magic-Angle-Spinning Solid-State NMR
Protonation, Tautomerization, and Rotameric Structure of Histidine: A Comprehensive Study by Magic-Angle-Spinning Solid-State NMR
Shenhui Li and Mei Hong
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja108943n/aop/images/medium/ja-2010-08943n_0010.gif
Journal of the American Chemical Society
DOI: 10.1021/ja108943n
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/FuFM0C9qHyE
Determination of Histidine Protonation States in Proteins by Fast Magic Angle Spinning NMR
Linear Mode
