This Article Full Text Full Text (PDF) Supplemental Material All Versions of this Article: biophysj.104.047266v1 biophysj.104.047266v2 87/4/2701    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Waner, M. J. Articles by Mascotti, D. P. Search for Related Content PubMed PubMed Citation Articles by Waner, M. J. Articles by Mascotti, D. P.

Thermal and Sodium Dodecylsulfate Induced Transitions of Streptavidin

Mark J. Waner ^*, Irina Navrotskaya , Amanda Bain , Edward Davis Oldham  and David P. Mascotti ^*

^* Department of Chemistry, John Carroll University, University Heights, Ohio 44118; Chemistry Department, College of Literature, Science, and Arts, University of Michigan, Ann Arbor, Michigan 48109-1055; Department of Chemistry, College of Wooster, Wooster, Ohio 44691; and Department of Chemistry, Lawrence University, Appleton, Wisconsin 54912

Correspondence: Address reprint requests to David P. Mascotti, E-mail: dmascotti{at}jcu.edu.

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.

This article has been cited by other articles:

				S.-C. Wu and S.-L. Wong Engineering Soluble Monomeric Streptavidin with Reversible Biotin Binding Capability J. Biol. Chem., June 17, 2005; 280(24): 23225 - 23231. [Abstract] [Full Text] [PDF]