Department of Chemistry "Ugo Schiff" and Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino (Florence), Italy.
Chem Rev. 2022 May 25;122(10):9468-9496. doi: 10.1021/acs.chemrev.1c00871. Epub 2022 Jan 13.
Thanks to recent improvements in NMR spectrometer hardware and pulse sequence design, modern C NMR has become a useful tool for biomolecular applications. The complete assignment of a protein can be accomplished by using C detected multinuclear experiments and it can provide unique information relevant for the study of a variety of different biomolecules including paramagnetic proteins and intrinsically disordered proteins. A wide range of NMR observables can be measured, concurring to the structural and dynamic characterization of a protein in isolation, as part of a larger complex, or even inside a living cell. We present the different properties of C with respect to H, which provide the rationale for the experiments developed and their application, the technical aspects that need to be faced, and the many experimental variants designed to address different cases. Application areas where these experiments successfully complement proton NMR are also described.
由于近年来 NMR 谱仪硬件和脉冲序列设计的改进，现代 C NMR 已成为生物分子应用的有用工具。通过使用 C 检测多核实验，可以完成蛋白质的完整分配，并且可以为研究各种不同的生物分子（包括顺磁蛋白和天然无序蛋白）提供相关的独特信息。可以测量广泛的 NMR 可观测值，这些可观测值有助于孤立的、更大复合物中的或甚至在活细胞内的蛋白质的结构和动力学特征的描述。我们介绍了 C 相对于 H 的不同性质，这些性质为开发的实验及其应用提供了依据，说明了需要面对的技术方面，以及为解决不同情况而设计的许多实验变体。还描述了这些实验成功补充质子 NMR 的应用领域。
