Thermal stability and binding energetics of thymidylate synthase ThyX

Krumova, Sashka; Todinova, Svetla; Tileva, Milena; Bouzhir-Sima, Latifa; Vos, Marten H.; Liebl, Ursula; Taneva, Stefka G.

doi:10.1016/j.ijbiomac.2016.05.083

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“…The integral of the excess heat capacity function is the enthalpy in this process. Thermodynamic parameters, such as temperature of unfolding ( T m ) and change in enthalpy, give huge information about the structure and functional parameters of the proteins, as well as about the nature of their interactions with other ligands or drug [ 3 – 5 ].…”

Section: Introductionmentioning

confidence: 99%

Calorimetric Study of Helix aspersa Maxima Hemocyanin Isoforms

Todinova

Raynova

Idakieva

2018

Journal of Analytical Methods in Chemistry

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The thermal unfolding of hemocyanin isoforms, β-HaH and αD+N-HaH, isolated from the hemolymph of garden snails Helix aspersa maxima, was studied by means of differential scanning calorimetry (DSC). One transition, with an apparent transition temperature (Tm) at 79.88°C, was detected in the thermogram of β-HaH in 20 mM HEPES buffer, containing 0.1 M NaCl, 5 mM CaCl2, and 5 mM MgCl2, pH 7.0, at scan rate of 1.0°C min−1. By means of successive annealing procedure, two individual transitions were identified in the thermogram of αD+N-HaH. Denaturation of both hemocyanins was found to be an irreversible process. The scan-rate dependence of the calorimetric profiles indicated that the thermal unfolding of investigated hemocyanins was kinetically controlled. The thermal denaturation of the isoforms β-HaH and αD+N-HaH was described by the two-state irreversible model, and parameters of the Arrhenius equation were calculated.

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Section: Introductionmentioning

confidence: 99%