The smooth myosin rod exhibits uniform structural stability along its length, suggesting it lacks a specialized region for force-generating helix-coil transitions under physiological conditions.
Challenges assumptions of localized instability in smooth myosin; leaves open physiological force-generation mechanisms in cardiovascular tissues.
Studies using differential scanning calorimetry indicated that the isolated rod domain of the pig stomach myosin undergoes a single reversible helix‐coil transition with a temperature midpoint of 325 K at physiological pH and ionic strength. Similar behaviour was observed for both the isolated LMM and SF‐2 fragments of the rod. The results suggest that the smooth myosin rod has rather uniform structural stability along its length, and is thus unlikely to contain a specialised region which undergoes a substantial force‐generating helix‐coil transition under physiological conditions.
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Cross et al. (1983) studied this question.
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