Accurate Determination of 1 H‐ 15 N Dipolar Couplings Using Inaccurate Settings of the Magic Angle in Solid‐State NMR Spectroscopy

2019 ◽  
Vol 131 (13) ◽  
pp. 4330-4334 ◽  
Author(s):  
Kai Xue ◽  
Max Mühlbauer ◽  
Salvatore Mamone ◽  
Riddhiman Sarkar ◽  
Bernd Reif
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Solid State Nmr ◽  
Accurate Determination ◽  
Dipolar Couplings ◽  
Magic Angle ◽  
Solid State Nmr Spectroscopy

scholarly journals Characterization of nucleosome sediments for protein interaction studies by solid-state NMR spectroscopy

2021 ◽  
Author(s):  
Ulric B. le Paige ◽  
ShengQi Xiang ◽  
Marco M. R. M. Hendrix ◽  
Yi Zhang ◽  
Markus Weingarth ◽  
...  
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Solid State Nmr ◽  
Magic Angle Spinning ◽  
Magic Angle ◽  
Dense Phase ◽  
Binding Studies ◽  
Nmr Studies ◽  
Solid State Nmr Spectroscopy ◽  
Wide Range

Abstract. Regulation of DNA-templated processes such as gene transcription and DNA repair depend on the interaction of a wide range of proteins to the nucleosome, the fundamental building block of chromatin. Both solution and solid-state NMR spectroscopy have become an attractive approach to study the dynamics and interactions of nucleosomes, despite their high molecular weight of ~200 kDa. For solid-state NMR (ssNMR) studies, dilute solutions of nucleosomes are converted to a dense phase by sedimentation or precipitation. Since nucleosomes are known to self-associate, these dense phases may induce extensive interactions between nucleosomes, which could interfere with protein binding studies. Here, we characterized the packing of nucleosomes in the dense phase created by sedimentation using NMR and small-angle x-ray scattering (SAXS) experiments. We found that nucleosome sediments are gels with variable degrees of solidity, have nucleosome concentration close to that found in crystals, and are stable for weeks under high-speed magic angle spinning (MAS). Furthermore, SAXS data recorded on recovered sediments indicate that there is no pronounced long-range ordering of nucleosomes in the sediment. Finally, we show that the sedimentation approach can also be used to study low affinity protein interactions with the nucleosome. Together, our results give new insights into the sample characteristics of nucleosome sediments for ssNMR studies and illustrate the broad applicability of sedimentation-based NMR studies.

scholarly journals 3D structure determination of amyloid fibrils using solid-state NMR spectroscopy

Methods ◽  
2018 ◽  
Vol 138-139 ◽  
pp. 26-38 ◽  
Author(s):  
Antoine Loquet ◽  
Nadia El Mammeri ◽  
Jan Stanek ◽  
Mélanie Berbon ◽  
Benjamin Bardiaux ◽  
...  
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Structure Determination ◽  
Solid State Nmr ◽  
Amyloid Fibrils ◽  
3D Structure ◽  
Solid State Nmr Spectroscopy ◽  
3D Structure Determination

scholarly journals Exploiting the Synergy of Powder X-ray Diffraction and Solid-State NMR Spectroscopy in Structure Determination of Organic Molecular Solids

2013 ◽  
Vol 117 (23) ◽  
pp. 12258-12265 ◽  
Author(s):  
Dmytro V. Dudenko ◽  
P. Andrew Williams ◽  
Colan E. Hughes ◽  
Oleg N. Antzutkin ◽  
Sitaram P. Velaga ◽  
...  
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Structure Determination ◽  
Solid State Nmr ◽  
Molecular Solids ◽  
X Ray Diffraction ◽  
X Ray ◽  
Solid State Nmr Spectroscopy

A unified heteronuclear decoupling strategy for magic-angle-spinning solid-state NMR spectroscopy

2015 ◽  
Vol 142 (18) ◽  
pp. 184201 ◽  
Author(s):  
Asif Equbal ◽  
Morten Bjerring ◽  
P. K. Madhu ◽  
Niels Chr. Nielsen
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Solid State Nmr ◽  
Magic Angle Spinning ◽  
Magic Angle ◽  
Solid State Nmr Spectroscopy ◽  
Angle Spinning
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