van de Ven F J, de Bruin S H, Hilbers C W
Eur J Biochem. 1983 Aug 15;134(3):429-38. doi: 10.1111/j.1432-1033.1983.tb07585.x.
A method for the large-scale isolation of ribosomal proteins is described avoiding pre-separation of 30-S and 50-S subunits. Five proteins isolated in this way were studied with high-resolution 1H NMR at 500 MHz. These are S21, L18, L25, L30 and L33. The results show that L18, L25 and L30 exhibit tertiary structure in solution and indications for secondary structure in S21 are found. Protein L33 appears to be a random coil. Several resonances in the 1H NMR spectra are assigned to particular protons of amino acid residues, e.g. the aromatic ring protons of tyrosines and histidines, and epsilon-protons of lysines.
描述了一种用于大规模分离核糖体蛋白的方法，该方法避免了30-S和50-S亚基的预分离。以这种方式分离出的五种蛋白质在500 MHz下用高分辨率1H NMR进行了研究。它们是S21、L18、L25、L30和L33。结果表明，L18、L25和L30在溶液中呈现三级结构，并且发现了S21中二级结构的迹象。蛋白质L33似乎是无规卷曲。1H NMR谱中的几个共振峰被指定为氨基酸残基的特定质子，例如酪氨酸和组氨酸的芳香环质子以及赖氨酸的ε-质子。
