Kime M J, Ratcliffe R G, Moore P B, Williams R J
Eur J Biochem. 1981 May 15;116(2):269-76. doi: 10.1111/j.1432-1033.1981.tb05329.x.
A highly folded form of the ribosomal protein L25 from Escherichia coli can be obtained from urea-denatured preparations. Proton NMR data show that this form of the molecule must have a compact, globular tertiary structure. Spectroscopically it is indistinguishable from L25 prepared by methods which avoid denaturing solvents. Thus L25 is a protein which can be reversibly denatured. The stability and solubility of the folded form of the protein are discussed and primary assignments made for a number of resonances in its NMR spectrum. The paper shows that this folded form of the protein can be characterised using NMR spectroscopy. High-resolution NMR spectroscopy provides a sensitive and general way for the characterisation of protein folds.
来自大肠杆菌的核糖体蛋白L25的一种高度折叠形式可从尿素变性制剂中获得。质子核磁共振数据表明，这种分子形式必定具有紧密的球状三级结构。从光谱学角度看，它与通过避免使用变性溶剂的方法制备的L25无法区分。因此，L25是一种可被可逆变性的蛋白质。文中讨论了该蛋白质折叠形式的稳定性和溶解性，并对其核磁共振谱中的一些共振峰进行了初步归属。本文表明，这种蛋白质的折叠形式可用核磁共振光谱进行表征。高分辨率核磁共振光谱为蛋白质折叠的表征提供了一种灵敏且通用的方法。
