Structure of myoglobin-sugar-water systems

This proposal is a continuation of our previous experiment on NIMROD (Rb 1520094), where we studied aqueous solutions of trehalose (33 wt% trehalose) as well as myoglobin in the same solution (25 wt% myoglobin). The results of these previous measurements are very interesting and show that water and trehalose are homogenously distributed with plenty of hydorogen bonding inbetween. For the tenary system it is evident that myoglobin is prefentially surrounded by wate and that trehalose in the remaining solution causes a remarkable structural ordering of the myoglobin molecules. The aim of this proposal is both to elucidate whether the results are unique for trehalose, or will be similar for another sugar, and to determine how the ordering of the myoglobin molecules, as well as the distibution of the sugar molecules, are affected by a lower protein concentration and/or another sugar.

本研究提案是对此前依托NIMROD（Rb 1520094）开展的实验的延续。此前的实验中，我们分别研究了海藻糖（trehalose）水溶液（海藻糖质量分数为33 wt%）以及该体系中肌红蛋白（myoglobin）的样品（肌红蛋白质量分数为25 wt%）。上述前期测量获得的结果颇具启发性，结果表明水分子与海藻糖分子分布均匀，二者之间存在大量氢键相互作用。针对该三元体系，实验结果清晰显示肌红蛋白优先被水分子包裹，而剩余溶液中的海藻糖可促使肌红蛋白分子形成显著的结构有序排列。本提案的研究目标分为两点：一是探明上述实验结果是否为海藻糖所独有，抑或是更换为其他糖类也可得到相似结果；二是明确当蛋白质浓度降低或更换糖类时，肌红蛋白分子的有序排列状态以及糖类分子的分布情况会受到何种影响。