Data on whole length myosin binding protein C stabilizes myosin S2 as measured by gravitational force spectroscopy
Rohit R. Singh,
James W. Dunn,
Motamed M. Qadan,
Nakiuda Hall,
Kathy K. Wang,
Douglas D. Root
Affiliations
Rohit R. Singh
Department of Biological Sciences, Division of Biochemistry and Molecular Biology, University of North Texas, Denton, TX 76203, United States
James W. Dunn
Department of Biological Sciences, Division of Biochemistry and Molecular Biology, University of North Texas, Denton, TX 76203, United States
Motamed M. Qadan
Department of Biological Sciences, Division of Biochemistry and Molecular Biology, University of North Texas, Denton, TX 76203, United States
Nakiuda Hall
Department of Biological Sciences, Division of Biochemistry and Molecular Biology, University of North Texas, Denton, TX 76203, United States
Kathy K. Wang
Department of Biological Sciences, Division of Biochemistry and Molecular Biology, University of North Texas, Denton, TX 76203, United States
Douglas D. Root
Corresponding author.; Department of Biological Sciences, Division of Biochemistry and Molecular Biology, University of North Texas, Denton, TX 76203, United States
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.
