Electrostatics play an important role in many aspects of protein chemistry. However, the accurate determination of side chain proton affinity in proteins by experiment and theory remains challenging. In recent years the field of nuclear magnetic resonance spectroscopy has advanced the way that protonation states are measured, allowing researchers to examine electrostatic interactions at an unprecedented level of detail and accuracy. Experiments are now in place that follow pH-dependent (13)C and (15)N chemical shifts as spatially close as possible to the sites of protonation, allowing all titratable amino acid side chains to be probed sequence specifically. The strong and telling response of carefully selected reporter nuclei allows individual titration events to be monitored. At the same time, improved frameworks allow researchers to model multiple coupled protonation equilibria and to identify the underlying pH-dependent contributions to the chemical shifts.

中文翻译：

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蛋白质静电学的当代NMR研究。

静电在蛋白质化学的许多方面起着重要作用。然而，通过实验和理论准确测定蛋白质中侧链质子亲和力仍然具有挑战性。近年来，核磁共振光谱学领域已经发展了质子态测量的方法，使研究人员能够以前所未有的细节和准确性检查静电相互作用。现在已经进行了实验，这些实验遵循pH依赖的（13）C和（15）N化学位移在空间上尽可能接近质子化的位置，从而允许对所有可滴定的氨基酸侧链进行特异性探测。精心选择的报告子核的强而有力的响应使得可以监测各个滴定事件。与此同时，