The Walter & Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, Victoria 3052, Australia.
J Magn Reson. 2011 Aug;211(2):243-7. doi: 10.1016/j.jmr.2011.05.013. Epub 2011 May 31.
Conformational or chemical exchange can cause significant sensitivity loss in NMR spectroscopy through resonance broadening for nuclear spins involved in these processes. While this effect may sometimes be alleviated by manipulating experimental conditions such as temperature, pH, and buffers, conditions optimal for all resonances are not always achievable. As a consequence, any means of recovering or minimizing this exchange-induced sensitivity loss is potentially of significant value in regaining information otherwise lost. We report the experimental observation of significant sensitivity gain for nuclear spins undergoing chemical exchange with solvent (water) at exchange rates ca 1-10 s(-1) in (1)H-(15)N correlation spectra of proteins acquired with band-selective pulses (the SOFAST-HMQC sequence).
构象或化学交换可通过涉及这些过程的核自旋的共振展宽导致 NMR 光谱中显著的灵敏度损失。虽然通过操纵实验条件（如温度、pH 值和缓冲液）有时可以减轻这种影响，但并非总是可以实现适用于所有共振的最佳条件。因此，任何恢复或最小化这种交换诱导的灵敏度损失的方法都有可能在恢复否则丢失的信息方面具有重要价值。我们报告了在使用带选择性脉冲（SOFAST-HMQC 序列）获得的蛋白质的 (1)H-(15)N 相关光谱中，对于以 1-10 s(-1)的交换速率与溶剂（水）发生化学交换的核自旋观察到的显著灵敏度增益的实验观察结果。
