Chien W J, Cheng S F, Chang D K
Institute of Chemistry, Academia Sinica, Taipei, Taiwan, Republic of China.
Anal Biochem. 1998 Nov 15;264(2):211-5. doi: 10.1006/abio.1998.2852.
The binding affinity of a protein kinase C substrate, neurogranin peptide NG(28-43), to a sodium dodecyl sulfate micelle was analyzed quantitatively by the diffusion coefficient (Da) of the peptide determined by pulsed field gradient NMR. By use of a two-state model, the fraction of the peptide in the bound state, and hence the binding constant, can be estimated. The obtained binding constant is within the same order of magnitude as those reported for similar systems using other techniques. The present method may be generalized to measure the formation constants of other peptide:micelle complexes.
通过脉冲场梯度核磁共振测定的神经颗粒素肽NG(28 - 43)（一种蛋白激酶C底物）的扩散系数（Da），对其与十二烷基硫酸钠胶束的结合亲和力进行了定量分析。利用双态模型，可以估算出处于结合状态的肽的比例以及结合常数。所获得的结合常数与使用其他技术报道的类似体系的结合常数处于同一数量级。本方法可推广用于测量其他肽:胶束复合物的形成常数。
