NUCLEAR MAGNETIC RESONANCE--NEW METHODS AND MOLECULAR STRUCTURE DETERMINATION

已开发出新的方法来提高蛋白质的灵敏度 通过将磁化从H2O溶剂转移到蛋白质来进行核磁共振。 使用脉冲场梯度和选择性脉冲来确保 在此期间，水的磁化强度保持在接近其平衡值的水平 整个实验。不稳定蛋白的交叉松弛和交换 然后，含有溶剂的质子会导致蛋白质信号强度增加。 对于大多数实验来说，增强的幅度在10%-50%之间 在H2O溶液中进行，在研究 溶剂与蛋白质的相互作用。这种新的方法被用来 为了证明HIV蛋白酶抑制剂DMP-323确实取代了 在缓蚀剂之间的其他复合体中观察到的保守的水分子 还有蛋白酶。

New methods have been developed which enhance the sensitivity of protein NMR by transferring magnetization from the H2O solvent to the protein. Pulsed field gradients and selective pulses are used to ensure that the water magnetization remains close to its equilibrium value during the entire experiment. Cross relaxation and exchange of labile protein protons with solvent then result in increased protein signal intensity. The enhancement ranges from 10-50% for most experiments that are conducted in H2O solution, to a three-fold enhancement when studying the interaction between solvent and protein. This new methodology was used to prove that the HIV protease inhibitor DMP-323 indeed displaces the conserved water molecule observed in other complexes between inhibitors and the protease.