The G-F transformation of actin is an endothermic process favored by higher temperatures, postulated as a transition of hydrated G-actin into dehydrated F-actin plus free water.
May influence actin dynamics during cardiac hypothermia; leaves open mechanistic validation in muscle models.
The effect of temperature on the equilibrium level of the G–F transformation of actin was investigated in solutions containing very low concentrations of salts. It is shown by physical methods that the G–F transformation is favored by higher temperatures and the F–G transformation by lower temperatures within the range 0–20°. On the basis of the assumption that the transformation is a reversible condensation, the critical actin concentration was obtained was a function of temperature in a given solvent. Analysis of results by a conventional method gives a positive enthalpy change of the order of 10 kcal./mole actin for the GF transformation. The overall reaction of the GF transformation is postulated as a transition of hydrated G–actin into dehydrated F–actin plus free water, with net increases in enthalpy and entropy. A chemical method is employed for determining G–actin concentration in equilibrium solutions. Almost all actin other than F–actin filaments must be G–actin (ATP‐actin).
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Asakura et al. (1960) studied this question.
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