Ideal Protein Materials with Genetic Code Expansion

Ryan Mehl
Assoicate Professor, Biochemistry and Biophysics Department at Oregon State Universtiy
Thursday, January 21, 2016 - 4:30pm
Fitzpatrick Center, Schiciano Auditorium B

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How would you like to modify the properties of your protein?

Genetic code expansion uses synthetic biology concepts to expand translation allowing for site-specific incorporation of non-canonical amino acids. The addition of a wide array of chemical functionalities into proteins provides unprecedented molecular control over proteins and therefore advances the capabilities of chemical biology and biomaterials.

Advances in genetic code expansion and its application to understanding oxidative stress and advancing biomaterials will be discussed. Access to genetic code expansion technology at the Oregon State University Unnatural Protein Facility will also be described.


Dr. Ryan Mehl is an Associate Professor of Biochemistry and Biophysics at Oregon State University. He is also the Director of the Unnatural Protein Facility at Oregon State University. Professor Mehl received his Ph.D. from Cornell University in 2001 and his B.S. from Moravian College in 1996 both in Chemistry. Professor Mehl research is focused on developing tools that enable the genetic encoding of modified amino acids and using them to study protein structure and function, to develop new technologies, and to answer questions of biomedical importance. I received my organic synthesis and mechanistic enzymology training under Tadhg Begley and my chemical biology/protein engineering training under Peter Schultz. Then, for 10 years I led a lab at Franklin and Marshall College, and working with undergraduates, used genetic code expansion to study the structural and catalytic properties of proteins with various noncanonical amino acids, as well as developing useful spectroscopic probes and bioorthogonal ligations. Over the past decade, I have solved many problems associated with producing proteins containing unnatural amino acids both in vivo and in vitro, and helped numerous colleagues at other institutions successfully establish the technology in their laboratories. I have recently relocated to Oregon State University, where I have expanded my research program and created an “Unnatural Protein Facility” dedicated to facilitating the use of unnatural amino acid incorporation methods While site-specifically incorporating new chemical functionality into proteins is important to advancing many feels protein research, moving these tools to the application stage so they can solve meaningful new biochemical problems is essential and the focus of the Facility. We are currently collaborating with the many labs to incorporate post-translational modifications and spectroscopic probes in the Facility.