Date of Award

Spring 2014

Document Type


Terms of Use

© 2014 Matthew R. Elkins. 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

First Advisor

Kathleen P. Howard


The influenza A M2 protein is 97-residues in length and homotetramerizes to form a proton channel across the viral membrane early in the influenza life cycle. M2 is also implicated in the formation and budding of new viral particles in a process proposed to require membrane cholesterol. A potential cholesterol recognition amino acid consensus (CRAC) immediately C-terminal to the M2 transmembrane domain is thought to mediate the M2-cholesterol interaction. However, the finer details of this interaction are largely unknown. Using site-directed spin labeling (SDSL) and electron paramagnetic resonance (EPR) spectroscopy, this research aims to gain a more detailed understanding of the interactions between M2 and cholesterol. EPR lineshapes using M2 constructs with and without the CRAC suggest that cholesterol influences M2 conformation and dynamics both by a direct interaction via the CRAC and indirectly by modifying the characteristics of the bilayer. Experiments investigating accessibility at individual CRAC residues indicate localization of cholesterol and suggest methods for further characterizing the apparent M2-cholesterol binding.

Included in

Chemistry Commons