Emily F. Ruff, Ph.D.

Kinase Regulation

There are over 500 protein kinase domains encoded by the human genome. Many are involved in signal transduction pathways that control aspects of cell development and proliferation. The focus of regulation for most Ser/Thr kinases is on the conformational transition between active and autoinhibited states. Each kinase has a unique set of allosteric mediators of this transition, including small molecule ligands, post-translational modifications, and protein-protein interactions. But for most kinases, little is known about how these conformational changes occur in solution. 

We have a variety of projects investigating the conformational regulation of kinases and pseudokinases, and how mutations of these enzymes can cause disease. For these projects we use a variety of biochemical techniques, including protein purification, site-directed mutagenesis, circular dichroism, kinetic activity assays, and fluorescence spectroscopy.

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Course-Based Research

Course-based research experiences (CUREs) can improve students' attitudes and retention in science. We are currently converting Winona State's CHEM 406 (Biochemistry I Lab) to a course-based research experience in which students purify and investigate disease-causing mutations of kinase domains. Students learn practical lab skills (like those listed above) as well as bioinformatics and molecular modeling skills, and they gain experience applying the scientific method.

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