Matheis G, Whitaker J R
Int J Biochem. 1984;16(8):867-73. doi: 10.1016/0020-711x(84)90145-9.
31P nuclear magnetic resonance (NMR) spectroscopy for characterizing the nature of covalently bound phosphate in proteins is relatively unexploited by the biochemist. 31P NMR chemical shifts of phosphate covalently bound to naturally occurring phosphoproteins, phosphorylated enzyme intermediates and chemically phosphorylated proteins have been compiled in this review. The chemical shifts (31P NMR) of selected reference compounds are reported to assist in the assignment of 31P resonances of phosphate covalently attached to proteins. 31P NMR chemical shifts of phosphate and phospho compounds non-covalently bound to selected proteins as well as the pH dependence of 31P NMR resonance have also been compiled.
用于表征蛋白质中共价结合磷酸盐性质的31P核磁共振（NMR）光谱，生物化学家对此研究相对较少。本综述汇编了与天然存在的磷蛋白、磷酸化酶中间体和化学磷酸化蛋白共价结合的磷酸盐的31P NMR化学位移。报道了选定参考化合物的化学位移（31P NMR），以协助确定与蛋白质共价连接的磷酸盐的31P共振峰。还汇编了与选定蛋白质非共价结合的磷酸盐和磷化合物的31P NMR化学位移，以及31P NMR共振的pH依赖性。
