Ethan Guth

Ethan Guth holds a Ph.D. in biochemistry from the University of Vermont College of Medicine and a B.S. from Goucher College. He joined the Norwich faculty in 2011, where he teaches Introduction to General Chemistry, Organic Chemistry, and Biochemistry I and II.

The central aim of his research to understand biological processes by elucidating the inner workings of biological machinery such as enzymes, which function as biological machines that accelerate the rate of chemical reactions. Understanding how these molecular machines perform their function allows scientists a “look under the hood” of biological processes and can provide profound insight into the basis of human health and disease.

Most recently, Guth has been collaborating on a project looking at the molecular basis for Usher Syndrome type IIIB, a genetic disorder characterized by postlingual deafness and retinal degeneration. That work has demonstrated that the protein produced from the genetic mutation associated with this disorder is functionally similar to the normal variant but less thermally stable. The results will help guide therapeutic avenues for treatment of this condition.

Ph.D., University of Vermont College of Medicine

B.S., Goucher College

My work has focused on the mechanism of enzyme action. These studies have helped to detail the mechanistic events of the catalytic cycle. More recently, I have extended the scope of my research to examine how differences in enzyme function effect cellular and organismal biology. My most recent work on the human histidyl-tRNA synthetase has examined the effect of a specific clinically relevant mutation that results in Usher syndrome. 

CH324 Biochemistry I
CH325 Biochemistry II
CH422 Senior Synthesis and Examination

Abbott JA, Livingston NM, Egri SB, Guth E, Francklyn CS. (2016) Characterization of aminoacyl-tRNA synthetase stability and substrate interaction by differential scanning fluorimetry. Methods doi: 10.1016/j.ymeth.2016.10.013

Özcelik D, Barandun J, Schmitz N, Sutter M, Guth E, Damberger FF, Allain FH, Ban N, Weber-Ban E. (2012) Structures of Pup ligase PafA and depupylase Dop from the prokaryotic ubiquitin-like modification pathway. Nature Communications doi: 10.1038/ncomms2009.

Guth EC, Thommen M, Weber-Ban E.  (2011)  Mycobacterial ubiquitin-like protein ligase PafA follows a two-step reaction pathway with a phosphorylated Pup intermediate. JBC, 286:4412-4419