کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1431052 | 1509189 | 2008 | 7 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Study of thermally and chemically unfolded conformations of bovine serum albumin by means of dynamic light scattering Study of thermally and chemically unfolded conformations of bovine serum albumin by means of dynamic light scattering](/preview/png/1431052.png)
The change of conformation of a bovine serum albumin (BSA) has been characterized using dynamic light scattering (DLS). Structural properties were investigated as a function of chemical denaturant concentrations and a temperature. In pure water, the protein keeps its native size at guanidine hydrochloride (GdmCl) concentrations below 1 M and behaves like an excluded volume chain above 4 M. A transition in structure and properties of the protein seems to occur around a GdmCl concentration of 1.7 M. Still, this protein forms an unfolded conformation in presence of 6 M of urea concentration and the value of the diffusive virial coefficient indicates that the interactions between the polypeptide chain and solvent are repulsive. The true value of the Tm = 43 °C, has obtained by linear extrapolation to 0 M GdmCl.
Journal: Materials Science and Engineering: C - Volume 28, Issues 5–6, 1 July 2008, Pages 594–600