Ron B. Wetzel, Ph.D., Director
B.S. Chemistry, Drexel University, 1969
Ph.D. Organic Chemistry, U. California, Berkeley, 1973
Postdoctoral, Max Planck Institute, Goettingen, 1973-75
Postdoctoral, Yale University, 1975-78
Senior Scientist, Genentech, 1978-89
Adjunct Professor, U. California, Santa Cruz, 1985-89
Research Fellow, SmithKline Beecham, 1989-95
Senior Research Fellow, Temple University, 1996-97
Professor, Department of Medicine, Graduate School of Medicine,
University of Tennessee, 1997-present
Adjunct Professor,
Department of Biochemistry and Cellular and Molecular Biology ,
University of Tennessee, 1997-present
Adjunct Professor, Department of Chemistry ,
University of Tennessee, 2001-present
Bio Sketch I was born in Hanover in south-central Pennsylvania in 1946 and received a BS in Chemistry from Drexel University in Philadelphia in 1969. My undergraduate research with Frank Davis on thermal reactions of the sulfur-nitrogen bond turned me on the research. My graduate work in George Kenyon's lab at UC Berkeley was investigating the mechanism of positional interchange at penta-coordinate phosphorus, a hot topic in those days due to the work of the Westheimer group on pseudorotation during phosphate ester hydrolysis. I spent two years in the lab of Fritz Eckstein at the Max Planck Institute of Experimental Medicine in Goettingen, Germany working on the synthesis and biological applications of nucleoside analogs. As a sidelight during my work in Goettingen, I was exposed to the sulfur chemistry of proteins, a subject that has remained dear to my heart throughout my research career. I spent three years in the lab of Dieter Soll in the Molecular Biophysics and Biochemistry Department at Yale University working on tRNA chemistry, enzymology and RNA sequencing. In 1978, I joined the fledgling biotech company, Genentech. Working on insulin and interferon projects, I soon got caught up in the challenge of managing the proper folding of recombinant proteins. In the early 80's at Genentech, Jeanne Perry and I completed on of the first successful protein engineering projects - introducing a disulfide bond into T4 lysozyme.
In this and later work looking at human gamma interferon, my group focused on the structural features of proteins that control stability against aggregation. At SmithKline, my group investigated the relationships between sequence, in vitro stability and bacterial inclusion body formation. My group at SmithKline made one of the first observations of the role thermodynamic stability plays in mediating mutational effects on amyloid formation by a globular protein (immunoglobulin light chain). We also demonstrated the critical role that proline residues can play in protecting protein sequences from amyloid formation and worked out methods for the management and measurement of Aß amyloid formation in vitro.
In 1997, I took advantage of the opportunity to set up an Alzheimer's research lab at the UT Medical Center. With the recent observation by several labs of the role of protein aggregates in polyglutamine expansion diseases, my group's research portfolio has expanded to include the study of the protein biophysics of Huntington's and related diseases. My group now divides its efforts between these two devastating neurodegenerative diseases.
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