Abstract
It is known that protein dimers form in a solution before proteinase K crystallization. Simulations of the dimer, i.e., a precursor cluster of the proteinase K crystal, at different temperatures, show that molecular dynamics methods make it possible to trace spatial and temporal changes in the internal structure of the crystal-forming dimer when heated to temperatures far from the denaturation. Based on the results of the modeling, the stability of the precursor cluster was evaluated at 19 temperatures (from 20 to 80 °C). An anomalous behavior of the dimer was found above 60 °C—a special temperature for the proteinase K (from Parengyodontium album) when the enzyme exhibits its maximal activity.
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