Molinari H, Ragona L, Varani L, Musco G, Consonni R, Zetta L, Monaco H L
Istituto Policattedra della Facoltà di Scienze, Universitá degli Studidi Verona, Italy.
FEBS Lett. 1996 Mar 4;381(3):237-43. doi: 10.1016/0014-5793(96)00100-7.
Bovine beta-LG (beta-lactoglobulin) has been studied under a variety of solution conditions by one- and two-dimensional NMR spectroscopy. At highly acidic pH (pH=2) and low ionic strength the protein is present in a monomeric form, exhibiting a highly structured beta-sheet core and less ordered regions as evidenced by both CD data and the NOESY spectra. Marginal protection was observed for most of the amide protons as a result of high conformational mobility. This structural state of beta-LG may be considered as an attractive model for a partially folded structure occurring late in the folding process of the protein.
牛β-乳球蛋白（β-乳球蛋白）已在多种溶液条件下通过一维和二维核磁共振光谱进行了研究。在高酸性pH值（pH = 2）和低离子强度下，该蛋白质以单体形式存在，如圆二色性（CD）数据和核Overhauser效应光谱（NOESY）所示，呈现出高度结构化的β-折叠核心和较少有序的区域。由于构象流动性高，大多数酰胺质子观察到边缘保护。β-乳球蛋白的这种结构状态可被视为蛋白质折叠过程后期出现的部分折叠结构的一个有吸引力的模型。
