scholarly journals Cover Picture: A Suite of Solid-State NMR Experiments for RNA Intranucleotide Resonance Assignment in a 21 kDa Protein-RNA Complex (Angew. Chem. Int. Ed. 38/2013)

2013 ◽  
Vol 52 (38) ◽  
pp. 9861-9861
Author(s):  
Alexander Marchanka ◽  
Bernd Simon ◽  
Teresa Carlomagno
2013 ◽  
Vol 125 (38) ◽  
pp. 10180-10185 ◽  
Author(s):  
Alexander Marchanka ◽  
Bernd Simon ◽  
Teresa Carlomagno

2020 ◽  
Vol 14 (2) ◽  
pp. 295-300 ◽  
Author(s):  
Tobias Schubeis ◽  
Tom S. Schwarzer ◽  
Tanguy Le Marchand ◽  
Jan Stanek ◽  
Kumar Tekwani Movellan ◽  
...  

2019 ◽  
Vol 58 (5) ◽  
pp. 445-465
Author(s):  
Jutta Hoffmann ◽  
Julia Ruta ◽  
Chaowei Shi ◽  
Kitty Hendriks ◽  
Veniamin Chevelkov ◽  
...  

2011 ◽  
Vol 133 (13) ◽  
pp. 4722-4725 ◽  
Author(s):  
Antoine Loquet ◽  
Guohua Lv ◽  
Karin Giller ◽  
Stefan Becker ◽  
Adam Lange

2021 ◽  
Author(s):  
Alons Lends ◽  
Melanie Berbon ◽  
Birgit Habenstein ◽  
Yusuke Nishiyama ◽  
Antoine Loquet

Solid-state NMR spectroscopy is a powerful technique to study insoluble and non-crystalline proteins and protein complexes at atomic resolution. The development of proton (1H) detection at fast magic-angle spinning (MAS) has considerably increased the analytical capabilities of the technique, enabling the acquisition of 1H-detected fingerprint experiments in few hours. Here an approach based on double-quantum (DQ) 13C spectroscopy, detected on 1H, is introduced at fast MAS (70 kHz) to perform the sequential assignment of insoluble proteins of small size, without any specific deuteration requirement. By combining two three-dimensional 1H detected experiments correlating a 13C DQ dimension respectively to its intra-residue and sequential 15N-1H pairs, a sequential walk through DQ (CA+CO) resonance is obtained. Our approach takes advantage of fast MAS to achieve an efficient sensitivity and the addition of a DQ dimension provides spectral features useful for the resonance assignment process.


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