Modeling NMR chemical shifts: surface charge representation of the electrostatic embedding potential modeling of crystalline intermolecular effects in 19F solid state NMR chemical shifts

2002 ◽  
Vol 602-603 ◽  
pp. 159-164 ◽  
Author(s):  
D. Solı́s ◽  
M.B. Ferraro ◽  
J.C. Facelli
2016 ◽  
Vol 22 (47) ◽  
pp. 16694-16694 ◽  
Author(s):  
Paolo Cerreia Vioglio ◽  
Luca Catalano ◽  
Vera Vasylyeva ◽  
Carlo Nervi ◽  
Michele R. Chierotti ◽  
...  

2019 ◽  
Vol 101 ◽  
pp. 31-37 ◽  
Author(s):  
Zhipeng Ke ◽  
Lauren E. Jamieson ◽  
Daniel M. Dawson ◽  
Sharon E. Ashbrook ◽  
Michael Bühl

Author(s):  
Hellmut Eckert ◽  
Kelly Moran ◽  
Deanna Franke ◽  
Christopher Hudalla

2019 ◽  
Vol 21 (27) ◽  
pp. 14992-15000 ◽  
Author(s):  
Martin Dračínský ◽  
Pablo Unzueta ◽  
Gregory J. O. Beran

A simple molecular correction improves significantly the accuracy of predictions of solid-state NMR chemical shifts.


2016 ◽  
Vol 22 (47) ◽  
pp. 16819-16828 ◽  
Author(s):  
Paolo Cerreia Vioglio ◽  
Luca Catalano ◽  
Vera Vasylyeva ◽  
Carlo Nervi ◽  
Michele R. Chierotti ◽  
...  

eLife ◽  
2017 ◽  
Vol 6 ◽  
Author(s):  
Simon Erlendsson ◽  
Kamil Gotfryd ◽  
Flemming Hofmann Larsen ◽  
Jonas Sigurd Mortensen ◽  
Michel-Andreas Geiger ◽  
...  

The Neurotransmitter:Sodium Symporters (NSSs) represent an important class of proteins mediating sodium-dependent uptake of neurotransmitters from the extracellular space. The substrate binding stoichiometry of the bacterial NSS protein, LeuT, and thus the principal transport mechanism, has been heavily debated. Here we used solid state NMR to specifically characterize the bound leucine ligand and probe the number of binding sites in LeuT. We were able to produce high-quality NMR spectra of substrate bound to microcrystalline LeuT samples and identify one set of sodium-dependent substrate-specific chemical shifts. Furthermore, our data show that the binding site mutants F253A and L400S, which probe the major S1 binding site and the proposed S2 binding site, respectively, retain sodium-dependent substrate binding in the S1 site similar to the wild-type protein. We conclude that under our experimental conditions there is only one detectable leucine molecule bound to LeuT.


2020 ◽  
Author(s):  
Marvin Grüne ◽  
Robert Luxenhofer ◽  
Dinu Iuga ◽  
Steven P. Brown ◽  
Ann-Christin Pöppler

We present <sup>14</sup>N-<sup>1</sup>H HMQC MAS NMR experiments in the solid state as a promising tool to study amorphous formulations. Poly(2-oxazoline) based polymer micelles loaded with different amounts of the cancer drug paclitaxel serve to highlight the possibilities offered by these experiments: While the very similar <sup>15</sup>N chemical shifts hamper a solid-state NMR characterization based on this nucleus, <sup>14</sup>N is a very versatile alternative. <sup>14</sup>N-<sup>1</sup>H HMQC experiments yield well-separated signals, which are spread over a large ppm range, provide information on the symmetry of the nitrogen environment and probe <sup>14</sup>N-<sup>1</sup>H through-space proximities.


Polymer ◽  
2005 ◽  
Vol 46 (25) ◽  
pp. 11737-11743 ◽  
Author(s):  
D.J. Harris ◽  
T.J. Bonagamba ◽  
M. Hong ◽  
K. Schmidt-Rohr

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