کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1986798 | 1540259 | 2013 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Thermal stability of matrix protein from Newcastle disease virus
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
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, ÎH(Tm), of 340 kcal molâ1, and the difference in heat capacity between the native and denatured states of the protein, ÎCp, of 5.1 kcal Kâ1 molâ1. 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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 61, October 2013, Pages 390-395
Journal: International Journal of Biological Macromolecules - Volume 61, October 2013, Pages 390-395
نویسندگان
Irene Sánchez Morán, Sara Cuadrado-Castano, Isabel Muñoz Barroso, Eduard Ya. Kostetsky, Galina Zhadan, Javier Gómez, Valery L. Shnyrov, Enrique Villar,