A differential scanning calorimetric study of Newcastle disease virus: identification of proteins involved in thermal transitions
1997
Shnyrov, V.L. | Zhadan, G.G. | Cobaleda, C. | Sagrera, A. | Munoz-Barroso, I. | Villar, E.
The irreversible thermal denaturation of Newcastle disease virus was investigated using different techniques including high-sensitivity differential scanning calorimetry, thermal gel analysis intrinsic fluorescence, and neuraminidase activity assays. Application of a successive annealing procedure to the scanning calorimetric endotherm of Newcastle disease virus furnished four elementary thermal transitions below the overall endotherm; these were further identified as coming from the denaturation of each viral protein. The shape of these transitions, as well as their scan-rate dependence, was explained by assuming that thermal denaturation takes place according to the kinetic scheme N k leads to D, where k is a first-order kinetic constant that changes with temperature, as given by the Arrhenius equation; N is the native state; and D is the denatured state. On the basis of this model, activation energy values were calculate The data obtained with the other methods used in this work support the proposed two-state kinetic model.
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