ArticleInternational journal of molecular sciences2026
Basal Heat Capacity of Skinned Skeletal Muscle with Selective Removal and Denaturation of Myoproteins: A Study with Differential Scanning Calorimetry.
Article in International journal of molecular sciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The specific heat capacity of skinned muscle in an adhering rigor solution was studied with differential scanning calorimetry (DSC) heating runs to search for a heat sink in the sarcomere of the muscle. To elucidate the contribution of major myoproteins to heat capacity, myosin and actin were partially removed by high-KCl and gelsolin treatments, respectively. Differential heat denaturation of myosin (together with α-actinin) and actin was induced to confirm their contributions. On the DSC curve, aside from the endothermic peaks representing ice melting and protein denaturation, the steady baseline level showed a significant increase in basal heat capacity in the presence of skinned muscle compared to the rigor solution alone. In the physiological temperature range from 10 to 25 °C, untreated skinned muscle in the native state (non-denatured) introduced an extra basal heat capacity of 0.4 J K
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