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Thermal stability of fish myosin
Institution:1. Unité de Nutrition, Service Endocrinologie-Diabétologie-Nutrition, CHU Rennes, Rennes, France;2. INRAE, INSERM, Univ Rennes, NuMeCan, Nutrition Metabolisms Cancer, Rennes, France;3. Laboratory “Movement Sport and Health Sciences” EA 7470, University of Rennes, ENS Rennes, 35170 Bruz, France;4. INRAE, PRISM Ani-Scans, St Gilles, Rennes, France;1. Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305, USA;2. Stanford Cardiovascular Institute, Stanford University School of Medicine, Stanford, CA 94305, USA;3. Department of Pediatrics (Cardiology), Stanford University School of Medicine, Stanford, CA 94305, USA;1. Department of Genetics, Harvard Medical School, New Research Building Room 256, 77 Avenue Louis Pasteur, Boston, MA 02115, USA;2. Department of Medicine, Brigham and Women’s Hospital, Harvard Medical School, 75 Francis Street, Boston, MA 02115, USA;3. Department of Genetics, Brigham and Women’s Hospital, Harvard Medical School, New Research Building Room 256, 77 Avenue Louis Pasteur, Boston, MA 02115, USA;4. Howard Hughes Medical Institute, 4000 Jones Bridge Road, Chevy Chase, MD 20815, USA
Abstract:
  • 1.1. Thermal stability of fish myosin has been studied by using differential scanning calorimetry (DSC) and circular dichroism (CD).
  • 2.2. The temperature range of the sharp decrease in α-helical content agreed very closely with that of the endothermic peaks.
  • 3.3. There was a high correlation between the enthalpy of denaturation (ΔH) and the decreasing quantity in α-helicity (Δh).
  • 4.4. The structure of fish myosins was much more unstable than that of rabbit.
  • 5.5. The instability of fish myosins was reflected in its rod moiety.
Keywords:
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