Mark Waner - Thermal and sodium dodecylsulfate induced transitions of Streptavidin

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      Publication Details (including relevant citation   information):

      Waner, M.J., Navrotskaya, I., Bain, A. Oldham, E. D. and   Mascotti, D. P., Biophys. J., 2004, 83, 2701-2713.

      Abstract:

      The strong specific binding of streptavidin (SA) to biotin is   utilized in numerous biotechnological applications. The SA   tetramer is also known to exhibit significant stability, even in   the presence of sodium dodecylsulfate (SDS). Despite its   importance, relatively little is known about the nature of the   thermal denaturation pathway for SA. This work uses a homogeneous   SA preparation to expand on the data of previous literature   reports, leading to the proposal of a model for temperature   induced structural changes in SA. Temperature dependent data were   obtained by SDS and native polyacrylamide gel electrophoresis   (PAGE), differential scanning calorimetry (DSC), and fluorescence   and ultraviolet (UV)-visible spectroscopy in the presence and   absence of SDS. In addition to the development of this model, it   is found that the major thermal transition of SA in 1% SDS is   reversible. Finally, although SA exhibits significant   precipitation at elevated temperatures in aqueous solution,   inclusion of SDS acts to prevent SA aggregation.

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