Welcome to the webpage of the Whitten Research Group.
We use experimental and computational techniques to investigate two issues:
- How intrinsically disordered proteins (IDPs) are utilized by the cell. IDPs have large regions that do not adopt stable structures, and yet these ID regions facilitate a range of biological tasks, such as mediating signaling pathways and regulating gene expression. It is not understood how or why nature uses ID for these purposes.
- The role of denatured states in determining how a protein folds. Because proteins have marginal stabilities, the tasks performed by folded proteins are often influenced by the myriad of partially folded and unfolded microstates that populate the protein conformational ensemble under native conditions. These microstates and their properties are important for elucidating the mechanisms that underlie folding pathways, protein stability, and protein misfolding diseases.
Links in the title bar give a current list of publications, a list of our presentations, a list of alums, and computational resources that include web-based apps used in our research.
Thank you for visiting.
Steven Whitten
Associate Professor
Department of Chemistry and Biochemistry
Texas State University
512-245-7893
steve.whitten@txstate.edu