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• W2163200767 abstract "The thermal stability of the matrix protein (M protein) of Newcastle disease virus (NDV) has been investigated using high-sensitivity differential scanning calorimetry (DSC) at pH 7.4. The thermal folding/unfolding of M protein at this pH value is a reversible process involving a highly cooperative transition between folded and unfolded monomers with a transition temperature (Tm) of 63 °C, an unfolding enthalpy, ΔH(Tm), of 340 kcal mol−1, and the difference in heat capacity between the native and denatured states of the protein, ΔCp, of 5.1 kcal K−1 mol−1. The heat capacity of the native state of the protein is in good agreement with the values calculated using a structure-based parameterization, whereas the calculated values for the hypothetical fully-unfolded state of the protein is higher than those determined experimentally. This difference between the heat capacity of denatured M protein and the heat capacity expected for an unstructured polypeptide of the same sequence, together with the data derived from the heat-induced changes in the steady-state fluorescence of the protein, indicates that the polypeptide chain maintains a significant amount of residual structure after thermal denaturation." @default.
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• W2163200767 date "2013-10-01" @default.
• W2163200767 modified "2023-10-01" @default.
• W2163200767 title "Thermal stability of matrix protein from Newcastle disease virus" @default.
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• W2163200767 doi "https://doi.org/10.1016/j.ijbiomac.2013.07.019" @default.
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