Institute of Organic Chemistry, University of Innsbruck, A- 6020, Innsbruck, Austria.
J Biomol NMR. 1999 Mar;13(3):213-21. doi: 10.1023/A:1008324721356.
A novel NMR experiment comprising adiabatic fast passage techniques for the measurement of heteronuclear self-relaxation rates in fully 15N-enriched proteins is described. Heteronuclear self-relaxation is monitored by performing adiabatic fast passage (AFP) experiments at variable adiabaticity (e.g., variation of RF spin-lock field intensity). The experiment encompasses gradient- selection and sensitivity-enhancement. It is shown that transverse relaxation rates derived with this method are in good agreement with the ones measured by the classical Carr-Purcell-Meiboom-Gill (CPMG) sequences. An application of this method to the study of the carboxyl-terminal LIM domain of quail cysteine and glycine-rich protein qCRP2(LIM2) is presented.
描述了一种新的 NMR 实验，该实验包含绝热快速通道技术，用于测量完全 15N 富集蛋白质中的异核自弛豫率。通过在不同的绝热性（例如，RF 自旋锁定场强度的变化）下执行绝热快速通道（AFP）实验来监测异核自弛豫。该实验包括梯度选择和灵敏度增强。结果表明，该方法得出的横向弛豫率与经典 Carr-Purcell-Meiboom-Gill（CPMG）序列测量的结果非常吻合。本文介绍了该方法在鹌鹑半胱氨酸和甘氨酸丰富蛋白 qCRP2（LIM2）羧基末端 LIM 结构域研究中的应用。
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