Unfolding of Concanavalin A by the Trifluoroethanol
The Stopped Flow method is used to analyze reactions occurred during the duration of several milliseconds
and several seconds meanwhile the CD measurement provides valuable information regarding the protein’s
secondary structures and environment of aromatic amino acids. Therefore, CD measurement with Stoppedflow
method provides one of the best techniques in analyzing the protein’s Unfolding and Refolding process.
Concanavalin A (derived from Jack bean) in natural state has abundant β-sheet structures, however, it is
known that its structure changes into the one with rich α-helix under trifluoroethanol (TFE) and its Unfolding
process has been reported also.
In this application, the model SFS-492 High-Speed Stopped-flow System was used to measure the Unfolding
process of Concanavalin A under TFE.
The Concanavalin A’s in pH2 hydrochloric acid gives a CD spectrum specific to β-sheet structure. In
contrast, in a solution with 50% of TFE added it has a CD spectrum specific to α-helix structures. As seen in
Figure 1, a big change from abundant β-sheet