scholarly journals Pushing the limits of sensitivity and resolution for natural abundance 43Ca NMR using ultra-high magnetic field (35.2 T)

2018 ◽  
Vol 54 (69) ◽  
pp. 9591-9594 ◽  
Author(s):  
Christian Bonhomme ◽  
Xiaoling Wang ◽  
Ivan Hung ◽  
Zhehong Gan ◽  
Christel Gervais ◽  
...  

Natural abundance 43Ca solid state NMR experiments are reported for the first time at ultra-high magnetic field (35.2 T) on a series of Ca-(pyro)phosphate and Ca-oxalate materials, which are of biological relevance in relation to biomineralization processes and the formation of pathological calcifications.

2006 ◽  
Vol 35 (9) ◽  
pp. 1058-1059 ◽  
Author(s):  
Yusuke Yamamoto ◽  
Miwa Murakami ◽  
Ryuichi Ikeda ◽  
Kenzo Deguchi ◽  
Masataka Tansho ◽  
...  

2015 ◽  
Vol 119 (49) ◽  
pp. 11847-11861 ◽  
Author(s):  
Alexandra Faucher ◽  
Victor V. Terskikh ◽  
Eric Ye ◽  
Guy M. Bernard ◽  
Roderick E. Wasylishen

2013 ◽  
Vol 27 (2) ◽  
pp. 760-763 ◽  
Author(s):  
Kanmi Mao ◽  
Gordon J. Kennedy ◽  
Stacey M. Althaus ◽  
Marek Pruski

2012 ◽  
Vol 26 (7) ◽  
pp. 4405-4412 ◽  
Author(s):  
Stacey M. Althaus ◽  
Kanmi Mao ◽  
Gordon J. Kennedy ◽  
Marek Pruski

2012 ◽  
Vol 50 (4) ◽  
pp. 289-294 ◽  
Author(s):  
Xiongchao Lin ◽  
Keiko Ideta ◽  
Jin Miyawaki ◽  
Yusuke Nishiyama ◽  
Isao Mochida ◽  
...  

2021 ◽  
Author(s):  
Alexander A. Malär ◽  
Laura A. Völker ◽  
Riccardo Cadalbert ◽  
Lauriane Lecoq ◽  
Matthias Ernst ◽  
...  

Temperature-dependent NMR experiments are often complicated by rather long magnetic-field equilibration times, for example occurring upon a change of sample temperature. We demonstrate that the fast temporal stabilization of the magnetic field can be achieved by actively stabilizing the temperature which allows to quantify the weak temperature dependence of the proton chemical shift which can be diagnostic for the presence of hydrogen bonds. Hydrogen bonding plays a central role in molecular recognition events from both fields, chemistry and biology. Their direct detection by standard structure determination techniques, such as X-ray crystallography or cryo-electron microscopy, remains challenging due to the difficulties of approaching the required resolution, on the order of 1 Å. We herein explore a spectroscopic approach using solid-state NMR to identify protons engaged in hydrogen bonds and explore the measurement of proton chemical-shift temperature coefficients. Using the examples of a phosphorylated amino acid and the protein ubiquitin, we show that fast Magic-Angle Spinning (MAS) experiments at 100 kHz yield sufficient resolution in proton-detected spectra to quantify the rather small chemical-shift changes upon temperature variations.<br>


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