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T. Michael Sabo, Ph.D.

CTRB-Rm 217
Assistant Professor of Medicine

More so than ever it is clear that processes essential to life, from enzyme catalysis to molecular recognition, are linked to the intrinsic motions of bio-molecular machines, in particular the fundamental machine of life: the protein. Such intrinsic motions manifest themselves in a conformational energy landscape, where any structural sub-state, be it functional or non-functional, is populated to an amount determined by that sub-state’s thermostability. From a therapeutic perspective, it is critical to ascertain which sub-state(s) to target with small molecule effectors and/or to stabilize through protein design efforts in order to adjust a bio-molecular system’s functionality by reshaping the distribution of the entire functional ensemble.
Thus, the overall focus of our research is to develop the tools that will be generally applicable for generating a comprehensive description of a bio-molecular functional ensemble and for characterizing the functional sub-states within that ensemble. The primary means for our research is nuclear magnetic resonance (NMR) spectroscopy, a technique that delivers many vital observables that are a beautiful blend of biology, chemistry, and physics. Current projects in the lab include, but are not limited to:
1. Investigating the linkage between conformational dynamics and functionality for the enzyme guanylate kinase
2. Utilizing NMR observables for generating functional state ensembles
3. Elucidating the relationship between slow and fast time-scale motions

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T. Michael Sabo, Ph.D.
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