title: Exploring various modulation-sideband recoupling conditions of SHA+ sequence at fast MAS.
abstract: We explore modulation-sideband recoupling conditions of the (13)C-(13)C Second-order Hamiltonian among Analogous nuclei plus pulse sequence (SHA+), and found that this sequence can be used in two different recoupling regimes. The first regime, νR>Δνiso(max), is recommended for broad-band recoupling to avoid any rotational resonance broadening. In this regime, the spinning speed should be only slightly larger than Δνiso(max), to obtain the best transfer efficiency. The second regime, νR<Δνiso(max), can be used to observe long-range constraints with lower spinning speed, which increases the transfer efficiency, and may allow using bigger rotors to increase the S/N ratio.
authors: Physics Department & Shanghai Key Laboratory of Magnetic Resonance, East China Normal University, Shanghai 200062, China; UCCS, Lille North of France University, Villeneuve d'Ascq 59652, France.
authors: Ming
authors: M
authors: Shen
authors: Qinghua
authors: Q
authors: Liu
authors: Julien
authors: J
authors: Trébosc
authors: Oliver
authors: O
authors: Lafon
authors: Yuichi
authors: Y
authors: Masuda
authors: K
authors: K
authors: Takegoshi
authors: Jean-Paul
authors: JP
authors: Amoureux
authors: Bingwen
authors: B
authors: Hu
authors: Qun
authors: Q
authors: Chen
mesh_terms: D016229:Amyloid beta-Peptides / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008958:Models, Molecular; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D013997:Time Factors
chemical_list: D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; C075222:amyloid beta-protein (1-42)
keywords: Bio-molecules; Fast MAS; Homo-nuclear correlation; Modulation sidebands; Solid-state NMR