Ghahramani Maryam, Yousefi Reza, Krivandin Alexey, Muranov Konstantin, Kurganov Boris, Moosavi-Movahedi Ali Akbar
Protein Chemistry Laboratory (PCL), Department of Biology, College of Sciences, Shiraz University, Shiraz, Iran.
Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Kosygin str. 4, Moscow 119991, Russia.
Data Brief. 2019 Dec 4;28:104922. doi: 10.1016/j.dib.2019.104922. eCollection 2020 Feb.
The α-Crystallin (α-Cry) functions as a molecular chaperone, preventing the formation of stress-induced protein aggregation which is important for maintenance of lens transparency. The kinetic data of Wt, R69C and D109H αB-Crys chaperone-like activity were obtained by UV-Vis spectroscopy in both thermal- and chemical-induced aggregation methods. The data were analyzed using physical parameters describing the aggregation process including * (the characteristic of the stage of nucleation), and (the characteristic of the stage of aggregate growth) and (the limiting value of the light scattering intensity). Parameter * is duration of the lag phase and the lower * value is associated with the higher rate of the nucleation stage. Also, the lower values of indicated the higher rate of aggregate growth stage. The change in parameter in the presence of chaperones can be connected with the change in the size of protein aggregates. These data are related to the research article entitled "" [1].
α-晶状体蛋白（α-Cry）作为一种分子伴侣，可防止应激诱导的蛋白质聚集形成，这对于维持晶状体透明度至关重要。通过紫外可见光谱法，在热诱导和化学诱导聚集方法中获得了野生型（Wt）、R69C和D109H αB-晶状体蛋白的分子伴侣样活性的动力学数据。使用描述聚集过程的物理参数对数据进行分析，这些参数包括*（成核阶段的特征）、 （聚集体生长阶段的特征）和 （光散射强度的极限值）。参数*是滞后阶段的持续时间，*值越低，成核阶段的速率越高。此外， 值越低，表明聚集体生长阶段的速率越高。在存在分子伴侣的情况下，参数 的变化可能与蛋白质聚集体大小的变化有关。这些数据与题为“”的研究文章相关[1]。
