Dobson C M, Lian L Y
Inorganic Chemistry Laboratory, University of Oxford, England.
FEBS Lett. 1987 Dec 10;225(1-2):183-7. doi: 10.1016/0014-5793(87)81154-7.
31P CP/MAS spectra have been obtained from 2'-CMP bound to ribonuclease A in the crystalline state. The chemical shift value is closely similar to that found in solution NMR studies under similar conditions, and corresponds to that of the dianionic state of the free compound. It is suggested that the NMR approach may be of general applicability for the comparison of the binding properties of small molecules to proteins in crystals and solution.
已获得处于结晶状态下与核糖核酸酶A结合的2'-胞苷一磷酸(2'-CMP)的31P交叉极化/魔角旋转(31P CP/MAS)光谱。化学位移值与在类似条件下溶液核磁共振(NMR)研究中发现的值非常相似,并且与游离化合物的二价阴离子状态相对应。有人提出,NMR方法可能普遍适用于比较小分子在晶体和溶液中与蛋白质的结合特性。