Published: Journal of Chromatographic Science, Volume 34, Number 2, February 1996, pp. 85-91
Capillary Electrophoretic Monitoring of the Folding and Unfolding
of b-Lactoglobulin B
Kevin R. Skelsey and Michelle M. Bushey
Capillary electrophoresis is used to monitor the change in peak mobility and shape that results from the folding and unfolding of b-lactoglobulin B. The protein is unfolded with denaturing solutions containing either urea or dithiothreitol or both denaturants. Samples are analyzed after varying exposure time to the denaturing solutions. When only urea is used as the denaturant, unfolded protein is refolded after dialysis, and the electrophoretic changes again suggest that a conformational change takes place as a function of time. The short analysis time required by capillary electrophoresis allows for observation of non-native conformations that are difficult to observe by conventional methods of electrophoresis or high-performance liquid chromatography.
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