The decay of RF-induced NMR spin polarization is characterized in terms of two separate processes, each with their own time constants. One process, called T 1, is responsible for the loss of resonance intensity following pulse excitation. The other process, called T 2, characterizes the width or broadness of resonances.

对于NMR不敏感的Pt原子化合物中所有的原子谱图峰模式为中心ddd裂分模式。 两边比较弱小的峰为自旋1/2的 引起的卫星峰。 注意到在90 MHz的谱仪上卫星峰几乎和中间峰一样尖锐。

2018年9月15日 · NMR resonance lines contain information on dynamic exchange processes, for example, the chemical exchange between two distinct conformations A and B in a biomolecule. In a relaxation dispersion experiment, chemical exchange during a fixed delay of the pulse sequence modulates the NMR signal intensities as a function of the amplitude of the ...

2012年3月1日 · The R2 (also Rxy) relaxation is the reciprocal of the transverse time constant (T2). T2 is the time constant that measures the decay of the transverse relaxation. Keeler, J. (2005) Understanding NMR Spectroscopy, 3rd ed., Wiley. [1] [2] This page was last modified 02:28, 1 March 2012. This page has been accessed 10,891 times.

2018年9月1日 · 一系列 NMR 实验现在可用于对蛋白质和核酸在从皮秒到数小时的整个生物学相关时间尺度内的运动进行采样。 在这里，我们专注于这些方法之一，弛豫分散，它解决了微到毫秒时间尺度上的动力学问题。 在这个时间尺度上发生的关键生物过程包括酶催化、配体结合和局部折叠。 换句话说，弛豫-弥散-分辨动力学通常与分子的功能密切相关，因此对结构生物化学家来说非常有趣。 该方法具有约 0.5% 的惊人灵敏度，可检测到任何其他生物物理方法都看不到的低种群 …

NMR relaxation methods enable the sampling and description of states that are otherwise invisible and enrich the annotation of static, ground state structures in the context of integrated structural biology. Developments of methods in the millisecond to second range reveals new insights for slow exchange and binding interactions

The R2 domain was stabilized by removing the cavity through a Val to Leu substitution at position 103 which significantly increased the thermostability of R2 (T m increased by 20 ° C) with ...

在这里，我们报告了一种可重复、准确且多功能的定量配体观察NMR测定，该测定可以使用横向弛豫率R 2作为可观察参数来确定低μM至低mM亲和力范围内片段的K d值。

Slow μs/ms dynamics involved in protein folding, binding, catalysis, and allostery are currently detected using NMR dispersion experiments such as CPMG (Carr−Purcell−Meiboom−Gill) or spin-lock R 1ρ. In these methods, protein dynamics are obtained by analyzing relaxation dispersion curves obtained from either changing the time spacing ...

2018年9月15日 · A battery of NMR experiments is now available to probe the motions of proteins and nucleic acids over the whole biologically relevant timescale from picoseconds to hours. Here we focus on one of these methods, relaxation dispersion, which resolves dynamics on the micro- to millisecond timescale.