SHA+脉冲序列用于g-C3N4样品15N-15N相关性的
收稿日期: 2015-03-11
修回日期: 2016-07-15
网络出版日期: 2016-09-05
基金资助
Large Instruments Open Foundation of East China Normal University, National Natural Science Foundation of China (21373086), National Science Fund of China for Excellent Young Scholars (21522303), Basic Research Project of Shanghai Science and Technology Committee (14JC1491000).
Probing 15N-15N Correlations in g-C3N4 Samples with Solid-State NMR SHA+ Pulse Sequence
Received date: 2015-03-11
Revised date: 2016-07-15
Online published: 2016-09-05
Supported by
Large Instruments Open Foundation of East China Normal University, National Natural Science Foundation of China (21373086), National Science Fund of China for Excellent Young Scholars (21522303), Basic Research Project of Shanghai Science and Technology Committee (14JC1491000).
利用固体核磁共振实验研究了15N标记的g-C3N4样品中的15N-15N空间相关性，在高场和魔角旋转条件下对比两种不同的脉冲序列PDSD和SHA+的实验效果．发现当某个氮上连有质子的时候，脉冲序列SHA+比PDSD可以更好地检测15N原子间的极化转移．该研究可以为材料科学领域，特别是含氮掺杂的碳材料，提供一种有价值的研究方法．
关键词： 固体核磁共振(SS-NMR); 同核相关; 长程相关; SHA+
闫晓静 , 胡炳文 . SHA+脉冲序列用于g-C3N4样品15N-15N相关性的[J]. 波谱学杂志, 2016 , 33(3) : 361 -367 . DOI: 10.11938/cjmr20160301
The performance of solid-state NMR proton-driven spin-diffusion (PDSD) and second-order Hamiltonian among analogous nuclei plus (SHA+) sequences for probing 15N-15N through-space correlations in 15N-labelled g-C3N4 samples were compared at high magnetic fields with moderate magic angle spinning (MAS) frequencies. It was found that, relative to the PDSD sequence, the SHA+ sequence is more efficient in terms of yielding polarization transfer between the 15N atoms as long as one of the nitrogen atoms bonds to protons. The results are useful in guiding the choice of solid-state nuclear magnetic resonance (SS-NMR) sequences for studying nitrogen-doped carbon-based materials.
[1] Castellani F, van Rossum B, Diehl A, et al. Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy[J]. Nature, 2002, 420(6 911): 98-102.
[2] Lange A, Becker S, Seidel K, et al. A concept for rapid protein-structure determination by solid-state NMR spectroscopy[J]. Angew Chem Int Ed Engl, 2005, 44(14): 2 089-2 092.
[3] Wasmer C, Lange A, van Melckebeke H, et al. Amyloid fibrils of the HET-s (218-289) Prion form a b solenoid with a triangular hydrophobic core[J]. Science, 2008, 319(5 869): 1 523-1 526.
[4] Lange A, Giller K, Hornig S, et al. Toxin-induced conformational changes in a potassium channel revealed by solid-state NMR[J]. Nature, 2006, 440(7 086): 959-962.
[5] Renault M, Cukkemane A, Baldus M. Solid-state NMR spectroscopy on complex biomolecules[J]. Angew Chem Int Ed Engl, 2010, 49(45): 8 346-8 357.
[6] Hong M, Zhang Y, Hu F H. Membrane protein structure and dynamics from NMR spectroscopy[J]. Annu Rev Phys Chem, 2012, 63: 1-24.
[7] Tycko R. Solid-state NMR studies of amyloid fibril structure[J]. Annu Rep Phys Chem, 2011, 62: 279-299.
[8] Takegoshi K, Nakamura S, Terao T. 13C-1H dipolar-assisted rotational resonance in magic-angle spinning NMR[J]. Chem Phys Lett, 2001, 344(5): 631-637.
[9] Takegoshi K, Nakamura S, Terao T. 13C-1H dipolar-driven 13C-13C recoupling without 13C rf irradiation in nuclear magnetic resonance of rotating solids[J]. J Chem Phys, 2003, 118(5): 2 325-2 341.
[10] Weingarth M, Masuda Y, Takegoshi K, et al. Sensitive 13C-13C correlation spectra of amyloid fibrils at very high spinning frequencies and magnetic fields[J]. J Biomol NMR, 2011, 50(2): 129-136.
[11] Weingarth M, Bodenhausen G, Tekely P. Broadband carbon-13 correlation spectra of micro crystalline proteins in very high-magnetic fields[J]. J Am Chem Soc, 2009, 131(39): 13 937-13 939.
[12] Weingarth M, Demco D E, Bodenhausen G, et al. Improved magnetization transfer in solid-state NMR with fast magic angle spinning[J]. Chem Phys Lett, 2009, 469(4, 5, 6): 342-348.
[13] Hu B W, Lafon O, Trébosc J, et al. Broad-band homo-nuclear correlations assisted by 1H irradiation for bio-molecules in very high magnetic field at fast and ultra-fast MAS frequencies[J]. J Magn Reson, 2011, 212(2): 320-329.
[14] Hu B W, Trébosc J, Lafon O, et al. Very-long-distance correlations in proteins revealed by solid-state NMR spectroscopy[J]. Chem Phys Chem, 2012, 13(16): 3 585-3 588.
[15] Scholz I, van Beek J D, Ernst M. Operator-based Floquet theory in solid-state NMR[J]. Solid State Nucl Magn Reson, 2010, 37(3, 4): 39-59.
[16] Leskes M, Akbey Ü, Oschkinat H, et al. Radio frequency assisted homo-nuclear recoupling, a Floquet description of homo-nuclear recoupling via surrounding hetero-nuclei in fully protonated to fully deuterated systems[J]. J Magn Reson, 2011, 209(2): 207-219.
[17] Jurgens B, Irran E, Senker J, et al. Melem (2,5,8-Triamino-tri-s-triazine), an important intermediate during condensation of melamine rings to Graphitic Carbon Nitride: synthesis, structure determination by X-ray powder diffractometry, solid-state NMR, and theoretical studies[J]. J Am Chem Soc, 2003, 125(34): 10 288-10 300.
[18] Bak M, Rasmussen J T, Nielsen N C. SIMPSON: A general simulation program for solid-state NMR spectroscopy[J]. J Magn Reson, 2000, 147(2): 296-330.
[19] Bak M, Nielsen N C. REPULSION: A novel approach to efficient powder averaging in solid-state NMR[J]. J Magn Reson, 1997, 125(1): 132-139.
[20] Fung B M, Khitrin A K, Ermolaev K. An improved broadband decoupling sequence for liquid crystals and solids[J]. J Magn Reson, 2000, 142(1): 97-101.
[21] Lotsch B V, Dçblinger M, Sehnert J, et al. Unmasking melon by a complementary approach employing electron diffraction, solid-state NMR spectroscopy, and theoretical calculations; structural characterization of a carbon nitride polymer[J]. Chem Eur J, 2007, 13(17): 4 969-4 980.
[22] Vosegaard T. Challenges in numerical simulations of solid-state NMR experiments: Spin exchange pulse sequences[J]. Solid State Nucl Magn Reson, 2010, 38(4): 77-83.
/
| 〈 |
|
〉 |