Graduate School of Frontier Sciences, The University of Tokyo, 5-1-5 Kashiwanoha, Kashiwa, Chiba, Japan.
Japan Synchrotron Radiation Research Institute, SPring-8, 1-1-1 Kouto, Sayo, Hyogo, Japan.
Sci Rep. 2017 Nov 1;7(1):13883. doi: 10.1038/s41598-017-14022-7.
Proteins in solution are conventionally considered macromolecules. Dynamic microscopic structures in supersaturated protein solutions have received increasing attention in the study of protein crystallisation and the formation of misfolded aggregates. Here, we present a method for observing rotational dynamic structures that can detect the interaction of nanoscale lysozyme protein networks via diffracted X-ray tracking (DXT). Our DXT analysis demonstrated that the rearrangement behaviours of lysozyme networks or clusters, which are driven by local density and concentration fluctuations, generate force fields on the femtonewton to attonewton (fN - aN) scale. This quantitative parameter was previously observed in our experiments on supersaturated inorganic solutions. This commonality provides a way to clarify the solution structures of a variety of supersaturated solutions as well as to control nucleation and crystallisation in supersaturated solutions.
溶液中的蛋白质通常被认为是大分子。在蛋白质结晶和错误折叠聚集体形成的研究中，过饱和蛋白质溶液中的动态微观结构受到了越来越多的关注。在这里，我们提出了一种观察旋转动态结构的方法，可以通过衍射 X 射线跟踪 (DXT) 来检测纳米级溶菌酶蛋白网络的相互作用。我们的 DXT 分析表明，溶菌酶网络或簇的重排行为是由局部密度和浓度波动驱动的，在飞牛顿到阿牛顿（fN-aN）尺度上产生力场。在我们对过饱和无机溶液的实验中，我们之前已经观察到了这个定量参数。这种共性为阐明各种过饱和溶液的溶液结构以及控制过饱和溶液中的成核和结晶提供了一种方法。
