Data on whole length myosin binding protein C stabilizes myosin S2 as measured by gravitational force spectroscopy

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...

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Bibliographic Details
Published in:Data in brief 2018-06, Vol.18, p.1099-1106
Main Authors: Singh, Rohit R., Dunn, James W., Qadan, Motamed M., Hall, Nakiuda, Wang, Kathy K., Root, Douglas D.
Format: Article
Language:English
Subjects:
Proteomics and Biochemistry
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Summary: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.
ISSN:2352-3409
2352-3409
DOI:10.1016/j.dib.2018.04.002