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Data on whole length myosin binding protein C stabilizes myosin S2 as measured by gravitational force spectroscopy.
Singh, Rohit R; Dunn, James W; Qadan, Motamed M; Hall, Nakiuda; Wang, Kathy K; Root, Douglas D.
Afiliación
  • Singh RR; Department of Biological Sciences, Division of Biochemistry and Molecular Biology, University of North Texas, Denton, TX 76203, United States.
  • Dunn JW; Department of Biological Sciences, Division of Biochemistry and Molecular Biology, University of North Texas, Denton, TX 76203, United States.
  • Qadan MM; Department of Biological Sciences, Division of Biochemistry and Molecular Biology, University of North Texas, Denton, TX 76203, United States.
  • Hall N; Department of Biological Sciences, Division of Biochemistry and Molecular Biology, University of North Texas, Denton, TX 76203, United States.
  • Wang KK; Department of Biological Sciences, Division of Biochemistry and Molecular Biology, University of North Texas, Denton, TX 76203, United States.
  • Root DD; Department of Biological Sciences, Division of Biochemistry and Molecular Biology, University of North Texas, Denton, TX 76203, United States.
Data Brief ; 18: 1099-1106, 2018 Jun.
Article en En | MEDLINE | ID: mdl-29900280
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.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Data Brief Año: 2018 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Países Bajos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Data Brief Año: 2018 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Países Bajos