在水中对肌红蛋白进行的质子核磁共振研究。
Proton nuclear magnetic resonance studies of myoglobin in H2O.
作者信息
Patel D J, Kampa L, Shulman R G, Yamane T, Wyluda B J
出版信息
Proc Natl Acad Sci U S A. 1970 Nov;67(3):1109-15. doi: 10.1073/pnas.67.3.1109.
Exchangeable hydrogens in proteins can be identified by comparison of nuclear magnetic resonance spectra obtained in H(2)O and in D(2)O. In oxymyoglobin and myoglobin we have been able to observe resonances of the NH protons of the two tryptophans, as well as one resonance from arginine and one from histidine in the range -10 to -15 ppm downfield from 3-(trimethylsilyl)propanesulfonic acid (sodium salt). These resonances have been identified by chemical modifications coupled with considerations of crystallographic structure and the dependence of the resonances on the species (sperm whale, porpoise, horse) from which the myglobin was obtained and on spin, pH, and temperature.
蛋白质中的可交换氢可通过比较在H₂O和D₂O中获得的核磁共振光谱来识别。在氧合肌红蛋白和肌红蛋白中，我们能够观察到两个色氨酸的NH质子的共振，以及在相对于3-（三甲基硅基）丙磺酸钠盐的化学位移为-10至-15 ppm范围内的一个精氨酸和一个组氨酸的共振。这些共振已通过化学修饰、结合晶体结构的考虑以及共振对肌红蛋白来源的物种（抹香鲸、鼠海豚、马）以及自旋、pH和温度的依赖性来确定。
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