With this award, the Chemistry of Life Processes Program in the Chemistry Division is funding Professor Gary A. Lorigan from the Department of Chemistry and Biochemistry at Miami University to investigate the structural and dynamic properties of a membrane protein known as pinholin. Novel powerful state-of-the-art techniques are used to study pinholin, which is an important membrane-bound protein that is directly involved in cell death. The last step of the virus infection cycle is cell death through lysis, the breakdown of the cell membrane. Professor Lorigan plan to develop the experimental procedures to characterize the structure and mechanism of the active and inactive forms of pinholin in a membrane. The pursuit allows graduate students, undergraduate students, and students from under-represented groups to obtain specialized training in cutting-edge Electron Paramagnetic Resonance (EPR) biophysical techniques. The new biophysical methods developed are useful generally to study a variety of different membrane protein systems. This research project also enables the development of a transformative STEM mentoring program called DUOS at Miami University that strengthens the synergy/interaction between graduate and undergraduate researchers to collaborate on a research project under the supervision of a faculty member in a Ph.D. granting department. One undergraduate/graduate student team from the Lorigan lab is scheduled to participate in this new program.
The research project is conducted to characterize the structure, topology, dynamics, and oligomerization state of the active and inactive forms of pinholin. Powerful CW-EPR and pulsed EPR spectroscopic techniques are used to investigate the different formations of pinholin. Multiple distances are to be measured between spin labels to provide important structural information on the pinholin embedded in a membrane. Information from this study should provide new insight into the pinholin mechanism and cell lysis, and provide novel methodology generally applicable to membrane proteins.
This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.
