Date of Award

Spring 2018

Document Type


Terms of Use

© 2018 Hayley E. Raymond. 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


Influenza A causes seasonal epidemics, and the possibility of another worldwide influenza A pandemic remains a public health concern. The influenza A M2 protein is implicated in the virus’s ability to bud and create new infectious virus particles. Specifically, the C-terminal region of the virus is required for viral budding, and this protein domain binds another influenza protein, M1. M2-M1 binding is critical to packaging the viral genome into new virions. To probe the region of M2 involved in viral budding and genome packing, this thesis studied the conformation of residues 60-70 of the C-terminus via site-directed spin label electron paramagnetic resonance (SDSL-EPR) spectroscopy. SDSL-EPR spectroscopy provided structural information about M2 reconstituted into 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine : 1-palmitoyl-2- oleoyl-sn-glycero-3-phospho-1-rac-glycerol (POPC:POPG) 4:1 lipid bilayers, a physiologically relevant environment. Mobility and membrane accessibility data revealed that residues 60-64 are associated with the membrane and are less mobile than residues 65-70. Residues 65-70 form a region with some periodic secondary structure, extending into the aqueous phase. A unique contribution of this thesis was the determination of the directionality of M2 insertion into the membrane via trypsin fragmentation and matrixassisted laser desorption ionization-mass spectrometry (MALDI-MS). According to current reconstitution protocols, M2 inserts into the membrane with no directionality, and both the N- and C-termini lie at the liposome exterior.

Included in

Chemistry Commons