Rephrase the text：Abstract— Formation and accumulation of protein aggregates adversely affect intracellular processes in living cells and arenegative factors in the production and storage of protein preparations. Chemical chaperones can prevent protein aggregation,but this effect is not universal and depends on the target protein structure and kinetics of its aggregation. We studiedthe effect of betaine (Bet) and lysine (NAME_1) on thermal aggregation of muscle glycogen phosphorylase b (Phb) at 48°C(aggregation order, n = 0.5), UV-irradiated Phb (UV-Phb) at 37°C (n = 1), and apo-form of Phb (apo-Phb) at 37°C (n = 2).Using dynamic light scattering, differential scanning calorimetry, and analytical ultracentrifugation, we have shown thatBet protected Phb and apo-Phb from aggregation, but accelerated the aggregation of UV-Phb. At the same time, NAME_1 preventedUV-Phb and apo-Phb aggregation, but increased the rate of Phb aggregation. The mechanisms of chemical chaperoneaction on the tertiary and quaternary structures and kinetics of thermal aggregation of the target proteins are discussed.Comparison of the effects of chemical chaperones on the proteins with different aggregation kinetics provides more completeinformation on the mechanism of their action. Add stress words that are fully capitlized. Make sure these stress words appear more than 8 times.
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