Differential scanning calorimetry offers a promising approach to investigate structural changes in the myosin head and F-actin due to their interaction.
Supports DSC for probing myosin-actin stability; leaves open translation to cardiac muscle mechanics in vivo.
The thermal unfolding of the myosin subfragment 1 (S1) and of filamentous actin (F-actin) in their strong complex obtained in the presence of ADP was studied by differential scanning calorimetry (DSC). It is shown that in the acto-S1 complexes S1 and F-actin melt separately, and thermal transitions of each protein can be easily followed. Interaction of S1 with F-actin significantly increases S1 thermal stability and also affects the thermal stability of F-actin. Although S1 unfolds at much lower temperature than F-actin, the molecules of S1 remain bound to F-actin even after full denaturation. Under these conditions S1 may induce cross-linking between actin filaments. It is concluded that DSC studies on the acto-S1 complexes offer a new and promising approach to investigate the structural changes which occur in the myosin head and in F-actin due to their interaction.
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Nikolaeva et al. (1996) studied this question.
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