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• W2023138601 abstract "Glutaredoxins (Grxs), redox-active proteins with a typical -CPYC motif at their active sites, are involved in redox-regulatory processes and antioxidant defenses. The human malarial parasite Plasmodium falciparum possess a classical glutaredoxin (PfGrx) as well as a number of Grx-like proteins. In the present study, we investigated the unfolding energetics and conformational stability of PfGrx, using isothermal guanidine hydrochloride-induced and pH-dependent thermal denaturation. Reversible unfolding can be modeled using a two-state transition between the native and unfolded states. The structural topology of the protein was stable over a wide pH range from 3.0 to 11.0. Although the protein was thermally stable, it exhibited a small free energy of 1.56 kcal mol−1 at 25 °C. The thermostability of PfGrx reached its maximum at pH 8.0, with a Tm of 76.2 °C and a ΔHm of 119 kcal mol−1. To elucidate the factors underlying the thermostability, a protein stability curve was generated. Maximum stability occurred at around 47 °C, where the ΔGDH2O value was 4.30 kcal mol−1. The high structural stability over a broad pH range, together with the capacity to endure very high temperatures, supports the notion that Grx can withstand a wide variety of conditions, allowing it to play a key role in cellular redox homeostasis. To the best of our knowledge, this work represents the first attempt to understand the energetic characteristics of a glutaredoxin in relation to accompanying structural changes." @default.
• W2023138601 created "2016-06-24" @default.
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• W2023138601 date "2010-03-01" @default.
• W2023138601 modified "2023-09-26" @default.
• W2023138601 title "Conformational stability and energetics of Plasmodium falciparum glutaredoxin" @default.
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• W2023138601 doi "https://doi.org/10.1016/j.biochi.2009.12.003" @default.
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