The trends vary with polymer family, but changes in activity are within threefold of buffer values. We also assessed activity in terms of volume occupancy, viscosity, and the overlap concentration (where polymers form an interwoven mesh). However, the effect decreases at higher concentrations, approaching, and, in some cases, falling below buffer values. At low concentrations, reductase activity increases relative to buffer and monomers, suggesting a macromolecular effect. Here, we report the effects of the synthetic polymer cosolutes Ficoll, dextran, and polyvinylpyrrolidone, and their respective monomers, sucrose, glucose, and 1-ethyl-2-pyrrolidone, on the activity of the 18-kDa monomeric enzyme, Escherichia coli dihydrofolate reductase. Studies that attempt to recreate the cellular interior in vitro often utilize synthetic polymers as crowding agents. Protein enzymes are the main catalysts in the crowded and complex cellular interior, but their activity is almost always studied in dilute buffered solutions.
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