通过重力光谱法测量的数据表明，全长肌球蛋白结合蛋白C可稳定肌球蛋白S2。
Data on whole length myosin binding protein C stabilizes myosin S2 as measured by gravitational force spectroscopy.
作者信息
Singh Rohit R, Dunn James W, Qadan Motamed M, Hall Nakiuda, Wang Kathy K, Root Douglas D
机构信息
Department of Biological Sciences, Division of Biochemistry and Molecular Biology, University of North Texas, Denton, TX 76203, United States.
出版信息
Data Brief. 2018 Apr 5;18:1099-1106. doi: 10.1016/j.dib.2018.04.002. eCollection 2018 Jun.
Data presented in this article relates to the research article entitled "Whole length myosin binding protein C stabilizes myosin subfragment-2 (S2) flexibility as measured by gravitational force spectroscopy." (Singh et al., 2018) [1]. The data exhibits the purified skeletal myosin binding protein C (MyBPC) from rabbit back muscle was of slow skeletal type confirmed by chromatography and in unphosphorylated state based on its isoelectric point (pI) by chromatofocussing. The competitive enzyme linked immunosorbent assay (cELISA) data displayed the site specificity of polyclonal anti-S2 antibody to myosin S2. This polyclonal antibody binding site corresponds to a familial hypertrophic cardiomyopathy (FHC) point mutation hotspot on myosin S2 illustrated in a figure of compiled data.
本文所呈现的数据与题为《全长肌球蛋白结合蛋白C稳定肌球蛋白亚片段2（S2）的柔韧性，通过重力光谱法测定》的研究文章相关（辛格等人，2018年）[1]。数据显示，从兔背部肌肉中纯化得到的骨骼肌肌球蛋白结合蛋白C（MyBPC）经色谱法确认为慢骨骼肌型，且根据其等电点通过聚焦色谱法确定处于未磷酸化状态。竞争性酶联免疫吸附测定（cELISA）数据显示了多克隆抗S2抗体对肌球蛋白S2的位点特异性。该多克隆抗体结合位点对应于肌球蛋白S2上的一个家族性肥厚性心肌病（FHC）点突变热点，在汇总数据图中有所展示。
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