Differential scanning calorimetry study of glycerinated rabbit psoas muscle fibres in intermediate state of ATP hydrolysis

Abstract

Background: Thermal denaturation experiments were extended to study the thermal behaviour of the main motor proteins (actin and myosin) in their native environment in striated muscle fibres. The interaction of actin with myosin in the highly organized muscle structure is affected by internal forces; therefore their altered conformation and interaction may differ from those obtained in solution. The energetics of long functioning intermediate states of ATP hydrolysis cycle was studied in muscle fibres by differential scanning calorimetry (DSC).

Cyclophosphamide treatment evoked side effects on skeletal muscle monitored by DSC

“…We could prove their similar effect in myofibrils, which are a real muscle model [27,28]. We have performed our measurements on muscle fibres too, and achieved similar temperature shift for all intermediate states of ATP hydrolysis in the higher temperature range [29][30][31][32][33][34][35][36][37][38][39].…”

Fractal dimension analysis and mathematical morphology of structural changes in actin filaments imaged by electron microscopy

“…The filament is quite flexible and the flexibility increases upon interaction with myosin, which is thought to play a key role in muscular contraction (Yanagida et al, 1984;Egelman and Orlova, 1995;Dergez et al, 2007;Vikhorev et al, 2008). Thus, these features of structure and dynamics characteristic to actin filament are our motivation of this study.…”

DSC and histological analysis of decellularized porcine biograft

“…Some small pretransition can be seen ~ 20 and 48 as well as at 54 °C. These two later peaks (which give only small enthalpy contribution) should have a myosin and actin origin on the basis of measurements performed on muscle protein solutions and skeletal muscle fibers [25][26][27][28][29][30][31]. In the literature, we have not found similar experiments performed on smooth muscles.…”