Date of Award

Spring 2013

Document Type


Terms of Use

© 2013 Richard Chen. All rights reserved. This work is freely available courtesy of the author. It may only be used for non-commercial, educational, and research purposes. For all other uses, including reproduction and distribution, please contact the copyright holder.

Degree Name

Bachelor of Arts


Chemistry & Biochemistry Department

First Advisor

Kathleen P. Howard


M2 is a 97-residue, multi-functional transmembrane protein that has been implicated in processes important to viral replication, such as proton conduction and viral budding of Influenza A. Due to experimental difficulties associated with the overexpression of membrane proteins, previous structural studies of M2 have focused on various synthetic truncated forms of the protein, which has lead to incomplete and sometimes inconsistent results. Therefore structural studies of the full-length M2 protein avoid the potential artifacts associated with truncations and provide more physiologically relevant data regarding the M2 protein. This research describes the successful overexpression, purification, spin-labeling, and reconstitution of the full-length M2 into lipid vesicles. Circular dichroism (CD) spectroscopy and electron paramagnetic resonance (EPR) spectroscopy are also utilized to characterize the full-length M2 protein in both micelles and lipid vesicles.

Included in

Chemistry Commons