No data available.
Please log in to see this content.
You have no subscription access to this content.
No metrics data to plot.
The attempt to load metrics for this article has failed.
The attempt to plot a graph for these metrics has failed.
The full text of this article is not currently available.
Handling the influence of chemical shift in amplitude-modulated heteronuclear dipolar recoupling solid-state NMR
R. Bhattacharyya, B. Key, H. Chen, A. S. Best, A. F. Hollenkamp, and C. P. Grey, “In situ NMR observation of the formation of metallic lithium microstructures in lithium batteries,” Nat. Mater. 9, 504–510 (2010).
D. K. Murray, J. W. Chang, and J. F. Haw, “Conversion of methyl halides to hydrocarbons on basic zeolites: A discovery by in situ NMR,” J. Am. Chem. Soc. 115, 4732–4741 (1993).
F. Castellani, B. van Rossum, A. Diehl, M. Schubert, K. Rehbein, and H. Oschkinat, “Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy,” Nature 420, 98–102 (2002).
A. Loquet, N. G. Sgourakis, R. Gupta, K. Giller, D. Riedel, C. Goosmann, C. Griesinger, M. Kolbe, D. Baker, S. Becker, and A. Lange, “Atomic model of the type III secretion system needle,” Nature 486, 276–279 (2012).
A. K. Schütz, T. Vagt, M. Huber, O. Y. Ovchinnikova, R. Cadalbert, J. Wall, P. Güntert, A. Böckmann, R. Glockshuber, and B. H. Meier, “Atomic-resolution three-dimensional structure of amyloid β fibrils bearing the Osaka mutation,” Angew. Chem., Int. Ed. 54, 331–335 (2015).
C. Wasmer, A. Lange, H. Van Melckebeke, A. B. Siemer, R. Riek, and B. H. Meier, “Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core,” Science 319, 1523–1526 (2008).
A. Krushelnitsky, D. Reichert, and K. Saalwächter, “Solid-state NMR approaches to internal dynamics of proteins: From picoseconds to microseconds and seconds,” Acc. Chem. Res. 46, 2028–2036 (2013).
J. R. Lewandowski, “Advances in solid-state relaxation methodology for probing site-specific protein dynamics,” Acc. Chem. Res. 46, 2018–2027 (2013).
P. Schanda and M. Ernst, “Studying dynamics by magic-angle spinning solid-state NMR spectroscopy: Principles and applications to biomolecules,” Prog. Nucl. Magn. Reson. Spectrosc. 96, 1–46 (2016).
E. R. Andrew, A. Bradbury, and R. G. Eades, “Removal of dipolar broadening of nuclear magnetic resonance spectra of solids by specimen rotation,” Nature 183, 1802–1803 (1959).
V. Agarwal, S. Penzel, K. Szekely, R. Cadalbert, E. Testori, A. Oss, J. Past, A. Samoson, M. Ernst, A. Böckmann, and B. H. Meier, “De novo 3D structure determination from sub-milligram protein samples by solid-state 100 kHz MAS NMR spectroscopy,” Angew. Chem., Int. Ed. 53, 12253–12256 (2014).
Z. Tošner, R. Andersen, B. Stevensson, M. Edén, N. C. Nielsen, and T. Vosegaard, “Computer-intensive simulation of solid-state NMR experiments using SIMPSON,” J. Magn. Reson. 246, 79–93 (2014).
N. Khaneja, T. Reiss, C. Kehlet, T. Schulte-Herbruggen, and S. J. Glaser, “Optimal control of coupled spin dynamics: Design of NMR pulse sequences by gradient ascent algorithms,” J. Magn. Reson. 172, 296–305 (2005).
C. T. Kehlet, A. C. Sivertsen, M. Bjerring, T. O. Reiss, N. Khaneja, S. J. Glaser, and N. C. Nielsen, “Improving solid-state NMR dipolar recoupling by optimal control,” J. Am. Chem. Soc. 126, 10202–10203 (2004).
O. Weintraub and S. Vega, “Floquet density matrices and effective Hamiltonians in magic-angle-spinning NMR spectroscopy,” J. Magn. Reson. A 105, 245–267 (1993).
A. B. Nielsen, K. O. Tan, R. Shankar, S. Penzel, R. Cadalbert, A. Samoson, B. H. Meier, and M. Ernst, “Theoretical description of RESPIRATION-CP,” Chem. Phys. Lett. 645, 150–156 (2016).
K. Basse, S. K. Jain, O. Bakharev, and N. C. Nielsen, “Efficient polarization transfer between spin-1/2 and 14N nuclei in solid-state MAS NMR spectroscopy,” J. Magn. Reson. 244, 85–89 (2014).
S. Jain, M. Bjerring, and N. C. Nielsen, “Efficient and robust heteronuclear cross-polarization for high-speed-spinning biological solid-state NMR spectroscopy,” J. Phys. Chem. Lett. 3, 703–708 (2012).
D. Wei, Ü. Akbey, B. Paaske, H. Oschkinat, B. Reif, M. Bjerring, and N. C. Nielsen, “Optimal 2H rf pulses and 2H-13C cross-polarization methods for solid-state 2H MAS NMR of perdeuterated proteins,” J. Phys. Chem. Lett. 2, 1289–1294 (2011).
K. Takegoshi, N. Miyazawa, K. Sharma, and P. K. Madhu, “Comparison among Magnus/Floquet/Fer expansion schemes in solid-state NMR,” J. Chem. Phys. 142, 134201 (2015).
K. O. Tan, M. Rajeswari, P. K. Madhu, and M. Ernst, “Asynchronous symmetry-based sequences for homonuclear dipolar recoupling in solid-state nuclear magnetic resonance,” J. Chem. Phys. 142, 065101 (2015).
J. T. Nielsen, M. Bjerring, M. D. Jeppesen, R. O. Pedersen, J. M. Pedersen, K. L. Hein, T. Vosegaard, T. Skrydstrup, D. E. Otzen, and N. C. Nielsen, “Unique identification of supramolecular structures in amyloid fibrils by solid-state NMR spectroscopy,” Angew. Chem., Int. Ed. 48, 2118–2121 (2009).
A. B. Nielsen, S. Jain, M. Ernst, B. H. Meier, and N. C. Nielsen, “Adiabatic Rotor-Echo-Short-Pulse-Irradiation mediated cross-polarization,” J. Magn. Reson. 237, 147–151 (2013).
Article metrics loading...
We present a theoretical analysis of the influence of chemical shifts on amplitude-modulated heteronuclear dipolar recoupling experiments in solid-state NMR spectroscopy. The method is demonstrated using the Rotor Echo Short Pulse IRrAdiaTION mediated Cross-Polarization (RESPIRATIONCP) experiment as an example. By going into the pulse sequence rf interaction frame and employing a quintuple-mode operator-based Floquet approach, we describe how chemical shift offset and anisotropic
chemical shift affect the efficiency of heteronuclear polarization transfer. In this description, it becomes transparent that the main attribute leading to non-ideal performance is a fictitious field along the rf field axis, which is generated from second-order cross terms arising mainly between chemical shift tensors and themselves. This insight is useful for the development of improved recoupling experiments. We discuss the validity of this approach and present quaternion calculations to determine the effective resonance conditions in a combined rf field and chemical shift offset interaction frame transformation. Based on this, we derive a broad-banded version of the RESPIRATIONCP experiment. The new sequence is experimentally verified using SNNFGAILSS amyloid
fibrils where simultaneous 15N → 13CO and 15N → 13Cα coherence transfer is demonstrated on high-field NMR instrumentation, requiring great offset stability.
Full text loading...
Most read this month