通过突破固有1H T1界限实现纳摩尔级蛋白质固态核磁共振。
Nanomole-scale protein solid-state NMR by breaking intrinsic 1HT1 boundaries.
作者信息
Wickramasinghe Nalinda P, Parthasarathy Sudhakar, Jones Christopher R, Bhardwaj Chhavi, Long Fei, Kotecha Mrignayani, Mehboob Shahila, Fung Leslie W-M, Past Jaan, Samoson Ago, Ishii Yoshitaka
机构信息
Department of Chemistry, University of Illinois at Chicago, 845 West Taylor Street, Chicago, IL 60607, USA.
出版信息
Nat Methods. 2009 Mar;6(3):215-8. doi: 10.1038/nmeth.1300. Epub 2009 Feb 8.
We present an approach that accelerates protein solid-state NMR 5-20-fold using paramagnetic doping to condense data-collection time (to approximately 0.2 s per scan), overcoming a long-standing limitation on slow recycling owing to intrinsic (1)H T(1) longitudinal spin relaxation. Using low-power schemes under magic-angle spinning at 40 kHz, we obtained two-dimensional (13)C-(13)C and (13)C-(15)N solid-state NMR spectra for several to tens of nanomoles of beta-amyloid fibrils and ubiquitin in 1-2 d.
我们提出了一种方法，通过顺磁掺杂将蛋白质固态核磁共振加速5至20倍，以缩短数据采集时间（至每次扫描约0.2秒），克服了由于固有氢核T1纵向自旋弛豫导致的长期存在的慢循环限制。在40千赫兹的魔角旋转下使用低功率方案，我们在1至2天内获得了几纳摩尔至几十纳摩尔的β-淀粉样纤维和泛素的二维碳-碳和碳-氮固态核磁共振谱。
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