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Intracellular water in Artemia cysts (brine shrimp)

机译:卤虫囊肿(盐水虾)中的细胞内水

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摘要

The dormant cysts of Artemia undergo cycles of hydration-dehydration without losing viability. Therefore, Artemia cysts serve as an excellent intact cellular system for studying the dynamics of water-protein interactions as a function of hydration. Deuterium spin-lattice (T1) and spin-spin (T2) relaxation times of water in cysts hydrated with D2O have been measured for hydrations between 1.5 and 0.1 g of D2O per gram of dry solids. When the relaxation rates (I/T1, I/T2) of 2H and 17O are plotted as a function of the reciprocal of hydration (1/H), an abrupt change in slope is observed near 0.6 g of D2O (or H2 17O)/gram of dry solids, the hydration at which conventional metabolism is activated in this system. The results have been discussed in terms of the two-site and multisite exchange models for the water-protein interaction as well as protein dynamics models. The 2H and 17O relaxation rates as a function of hydration show striking similarities to those observed for anisotropic motion of water molecules in protein crystals.It is suggested here that although the simple two-site exchange model or n-site exchange model could be used to explain our data at high hydration levels, such models are not adequate at low hydration levels (<0.6 g H2O/g) where several complex interactions between water and proteins play a predominant role in the relaxation of water nuclei. We further suggest that the abrupt change in the slope of I/T1 as a function of hydration in the vicinity of 0.6 g H2O/g is due to a change in water-protein interactions resulting from a variation in the dynamics of protein motion.
机译:卤虫休眠的囊肿经过水合脱水循环而不会丧失活力。因此,卤虫囊肿是研究水-蛋白质相互作用随水合作用的动力学的极好的完整细胞系统。对于每克干固体1.5至0.1克D2O的水合作用,已测量了在用D2O水化的囊中氘的自旋晶格(T1)和自旋自旋(T2)弛豫时间。当 2 H和 17 O的弛豫率(I / T1,I / T2)作为水合倒数(1 / H)的函数绘制时,在每克干固体0.6 g D2O(或H2 17 O)附近观察到斜率的突然变化,在该系统中,常规代谢被水化。已经针对水-蛋白质相互作用的两点和多点交换模型以及蛋白质动力学模型讨论了结果。作为水合作用的 2 H和 17 O弛豫速率与观察到的蛋白质晶体中水分子的各向异性运动显示出惊人的相似之处。简单的两点交换模型或n点交换模型可用于解释高水合水平下的数据,这种模型在低水合水平(<0.6 g H2O / g)下不足,因为水和蛋白质之间会发生一些复杂的相互作用在水核松弛中起主要作用。我们进一步建议,在0.6 g H2O / g附近,I / T1斜率的突然变化是水合作用的函数,这是由于蛋白质运动动态变化引起的水-蛋白质相互作用的变化。

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