van Rossum Barth-Jan, Castellani Federica, Pauli Jutta, Rehbein Kristina, Hollander J, de Groot Huub J M, Oschkinat Hartmut
Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle Str. 10, D-13125, Berlin, Germany.
J Biomol NMR. 2003 Mar;25(3):217-23. doi: 10.1023/a:1022819921584.
In this paper, we present a strategy for the (1)H(N) resonance assignment in solid-state magic-angle spinning (MAS) NMR, using the alpha-spectrin SH3 domain as an example. A novel 3D triple resonance experiment is presented that yields intraresidue H(N)-N-C(alpha) correlations, which was essential for the proton assignment. For the observable residues, 52 out of the 54 amide proton resonances were assigned from 2D ((1)H-(15)N) and 3D ((1)H-(15)N-(13)C) heteronuclear correlation spectra. It is demonstrated that proton-driven spin diffusion (PDSD) experiments recorded with long mixing times (4 s) are helpful for confirming the assignment of the protein backbone (15)N resonances and as an aid in the amide proton assignment.
在本文中，我们以α-血影蛋白SH3结构域为例，展示了一种用于固态魔角旋转（MAS）核磁共振中（1）H（N）共振归属的策略。提出了一种新颖的三维三重共振实验，该实验可产生残基内H（N）-N-C（α）相关性，这对于质子归属至关重要。对于可观测的残基，从二维（（1）H-（15）N）和三维（（1）H-（15）N-（13）C）异核相关谱中归属了54个酰胺质子共振中的52个。结果表明，采用长混合时间（4 s）记录的质子驱动自旋扩散（PDSD）实验有助于确认蛋白质主链（15）N共振的归属，并辅助酰胺质子的归属。
